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+anno_start	anno_end	anno_text	entity_type	sentence	section
+0	27	Structural characterization	experimental_method	Structural characterization of encapsulated ferritin provides insight into iron storage in bacterial nanocompartments	TITLE
+31	43	encapsulated	protein_state	Structural characterization of encapsulated ferritin provides insight into iron storage in bacterial nanocompartments	TITLE
+44	52	ferritin	protein_type	Structural characterization of encapsulated ferritin provides insight into iron storage in bacterial nanocompartments	TITLE
+75	79	iron	chemical	Structural characterization of encapsulated ferritin provides insight into iron storage in bacterial nanocompartments	TITLE
+91	100	bacterial	taxonomy_domain	Structural characterization of encapsulated ferritin provides insight into iron storage in bacterial nanocompartments	TITLE
+101	117	nanocompartments	complex_assembly	Structural characterization of encapsulated ferritin provides insight into iron storage in bacterial nanocompartments	TITLE
+0	9	Ferritins	protein_type	Ferritins are ubiquitous proteins that oxidise and store iron within a protein shell to protect cells from oxidative damage.	ABSTRACT
+57	61	iron	chemical	Ferritins are ubiquitous proteins that oxidise and store iron within a protein shell to protect cells from oxidative damage.	ABSTRACT
+79	84	shell	structure_element	Ferritins are ubiquitous proteins that oxidise and store iron within a protein shell to protect cells from oxidative damage.	ABSTRACT
+26	35	structure	evidence	We have characterized the structure and function of a new member of the ferritin superfamily that is sequestered within an encapsulin capsid.	ABSTRACT
+72	80	ferritin	protein_type	We have characterized the structure and function of a new member of the ferritin superfamily that is sequestered within an encapsulin capsid.	ABSTRACT
+123	133	encapsulin	protein	We have characterized the structure and function of a new member of the ferritin superfamily that is sequestered within an encapsulin capsid.	ABSTRACT
+18	30	encapsulated	protein_state	We show that this encapsulated ferritin (EncFtn) has two main alpha helices, which assemble in a metal dependent manner to form a ferroxidase center at a dimer interface.	ABSTRACT
+31	39	ferritin	protein_type	We show that this encapsulated ferritin (EncFtn) has two main alpha helices, which assemble in a metal dependent manner to form a ferroxidase center at a dimer interface.	ABSTRACT
+41	47	EncFtn	protein	We show that this encapsulated ferritin (EncFtn) has two main alpha helices, which assemble in a metal dependent manner to form a ferroxidase center at a dimer interface.	ABSTRACT
+57	75	main alpha helices	structure_element	We show that this encapsulated ferritin (EncFtn) has two main alpha helices, which assemble in a metal dependent manner to form a ferroxidase center at a dimer interface.	ABSTRACT
+97	112	metal dependent	protein_state	We show that this encapsulated ferritin (EncFtn) has two main alpha helices, which assemble in a metal dependent manner to form a ferroxidase center at a dimer interface.	ABSTRACT
+130	148	ferroxidase center	site	We show that this encapsulated ferritin (EncFtn) has two main alpha helices, which assemble in a metal dependent manner to form a ferroxidase center at a dimer interface.	ABSTRACT
+154	169	dimer interface	site	We show that this encapsulated ferritin (EncFtn) has two main alpha helices, which assemble in a metal dependent manner to form a ferroxidase center at a dimer interface.	ABSTRACT
+0	6	EncFtn	protein	EncFtn adopts an open decameric structure that is topologically distinct from other ferritins.	ABSTRACT
+17	21	open	protein_state	EncFtn adopts an open decameric structure that is topologically distinct from other ferritins.	ABSTRACT
+22	31	decameric	oligomeric_state	EncFtn adopts an open decameric structure that is topologically distinct from other ferritins.	ABSTRACT
+32	41	structure	evidence	EncFtn adopts an open decameric structure that is topologically distinct from other ferritins.	ABSTRACT
+84	93	ferritins	protein_type	EncFtn adopts an open decameric structure that is topologically distinct from other ferritins.	ABSTRACT
+6	12	EncFtn	protein	While EncFtn acts as a ferroxidase, it cannot mineralize iron.	ABSTRACT
+23	34	ferroxidase	protein_type	While EncFtn acts as a ferroxidase, it cannot mineralize iron.	ABSTRACT
+57	61	iron	chemical	While EncFtn acts as a ferroxidase, it cannot mineralize iron.	ABSTRACT
+16	26	encapsulin	protein	Conversely, the encapsulin shell associates with iron, but is not enzymatically active, and we demonstrate that EncFtn must be housed within the encapsulin for iron storage.	ABSTRACT
+27	32	shell	structure_element	Conversely, the encapsulin shell associates with iron, but is not enzymatically active, and we demonstrate that EncFtn must be housed within the encapsulin for iron storage.	ABSTRACT
+49	53	iron	chemical	Conversely, the encapsulin shell associates with iron, but is not enzymatically active, and we demonstrate that EncFtn must be housed within the encapsulin for iron storage.	ABSTRACT
+62	86	not enzymatically active	protein_state	Conversely, the encapsulin shell associates with iron, but is not enzymatically active, and we demonstrate that EncFtn must be housed within the encapsulin for iron storage.	ABSTRACT
+112	118	EncFtn	protein	Conversely, the encapsulin shell associates with iron, but is not enzymatically active, and we demonstrate that EncFtn must be housed within the encapsulin for iron storage.	ABSTRACT
+145	155	encapsulin	protein	Conversely, the encapsulin shell associates with iron, but is not enzymatically active, and we demonstrate that EncFtn must be housed within the encapsulin for iron storage.	ABSTRACT
+160	164	iron	chemical	Conversely, the encapsulin shell associates with iron, but is not enzymatically active, and we demonstrate that EncFtn must be housed within the encapsulin for iron storage.	ABSTRACT
+5	15	encapsulin	protein	This encapsulin nanocompartment is widely distributed in bacteria and archaea and represents a distinct class of iron storage system, where the oxidation and mineralization of iron are distributed between two proteins.	ABSTRACT
+16	31	nanocompartment	complex_assembly	This encapsulin nanocompartment is widely distributed in bacteria and archaea and represents a distinct class of iron storage system, where the oxidation and mineralization of iron are distributed between two proteins.	ABSTRACT
+57	65	bacteria	taxonomy_domain	This encapsulin nanocompartment is widely distributed in bacteria and archaea and represents a distinct class of iron storage system, where the oxidation and mineralization of iron are distributed between two proteins.	ABSTRACT
+70	77	archaea	taxonomy_domain	This encapsulin nanocompartment is widely distributed in bacteria and archaea and represents a distinct class of iron storage system, where the oxidation and mineralization of iron are distributed between two proteins.	ABSTRACT
+113	117	iron	chemical	This encapsulin nanocompartment is widely distributed in bacteria and archaea and represents a distinct class of iron storage system, where the oxidation and mineralization of iron are distributed between two proteins.	ABSTRACT
+176	180	iron	chemical	This encapsulin nanocompartment is widely distributed in bacteria and archaea and represents a distinct class of iron storage system, where the oxidation and mineralization of iron are distributed between two proteins.	ABSTRACT
+0	4	Iron	chemical	Iron is essential for life as it is a key component of many different enzymes that participate in processes such as energy production and metabolism.	ABSTRACT
+9	13	iron	chemical	However, iron can also be highly toxic to cells because it readily reacts with oxygen.	ABSTRACT
+79	85	oxygen	chemical	However, iron can also be highly toxic to cells because it readily reacts with oxygen.	ABSTRACT
+31	35	iron	chemical	To balance the cell’s need for iron against its potential damaging effects, organisms have evolved iron storage proteins known as ferritins that form cage-like structures.	ABSTRACT
+99	120	iron storage proteins	protein_type	To balance the cell’s need for iron against its potential damaging effects, organisms have evolved iron storage proteins known as ferritins that form cage-like structures.	ABSTRACT
+130	139	ferritins	protein_type	To balance the cell’s need for iron against its potential damaging effects, organisms have evolved iron storage proteins known as ferritins that form cage-like structures.	ABSTRACT
+150	170	cage-like structures	structure_element	To balance the cell’s need for iron against its potential damaging effects, organisms have evolved iron storage proteins known as ferritins that form cage-like structures.	ABSTRACT
+4	13	ferritins	protein_type	The ferritins convert iron into a less reactive form that is mineralised and safely stored in the central cavity of the ferritin cage and is available for cells when they need it.	ABSTRACT
+22	26	iron	chemical	The ferritins convert iron into a less reactive form that is mineralised and safely stored in the central cavity of the ferritin cage and is available for cells when they need it.	ABSTRACT
+98	112	central cavity	site	The ferritins convert iron into a less reactive form that is mineralised and safely stored in the central cavity of the ferritin cage and is available for cells when they need it.	ABSTRACT
+120	128	ferritin	protein_type	The ferritins convert iron into a less reactive form that is mineralised and safely stored in the central cavity of the ferritin cage and is available for cells when they need it.	ABSTRACT
+26	35	ferritins	protein_type	Recently, a new family of ferritins known as encapsulated ferritins have been found in some microorganisms.	ABSTRACT
+45	57	encapsulated	protein_state	Recently, a new family of ferritins known as encapsulated ferritins have been found in some microorganisms.	ABSTRACT
+58	67	ferritins	protein_type	Recently, a new family of ferritins known as encapsulated ferritins have been found in some microorganisms.	ABSTRACT
+92	106	microorganisms	taxonomy_domain	Recently, a new family of ferritins known as encapsulated ferritins have been found in some microorganisms.	ABSTRACT
+6	15	ferritins	protein_type	These ferritins are found in bacterial genomes with a gene that codes for a protein cage called an encapsulin.	ABSTRACT
+29	38	bacterial	taxonomy_domain	These ferritins are found in bacterial genomes with a gene that codes for a protein cage called an encapsulin.	ABSTRACT
+99	109	encapsulin	protein	These ferritins are found in bacterial genomes with a gene that codes for a protein cage called an encapsulin.	ABSTRACT
+13	22	structure	evidence	Although the structure of the encapsulin cage is known to look like the shell of a virus, the structure that the encapsulated ferritin itself forms is not known.	ABSTRACT
+30	40	encapsulin	protein	Although the structure of the encapsulin cage is known to look like the shell of a virus, the structure that the encapsulated ferritin itself forms is not known.	ABSTRACT
+72	77	shell	structure_element	Although the structure of the encapsulin cage is known to look like the shell of a virus, the structure that the encapsulated ferritin itself forms is not known.	ABSTRACT
+83	88	virus	taxonomy_domain	Although the structure of the encapsulin cage is known to look like the shell of a virus, the structure that the encapsulated ferritin itself forms is not known.	ABSTRACT
+94	103	structure	evidence	Although the structure of the encapsulin cage is known to look like the shell of a virus, the structure that the encapsulated ferritin itself forms is not known.	ABSTRACT
+113	125	encapsulated	protein_state	Although the structure of the encapsulin cage is known to look like the shell of a virus, the structure that the encapsulated ferritin itself forms is not known.	ABSTRACT
+126	134	ferritin	protein_type	Although the structure of the encapsulin cage is known to look like the shell of a virus, the structure that the encapsulated ferritin itself forms is not known.	ABSTRACT
+25	35	encapsulin	protein	It is also not clear how encapsulin and the encapsulated ferritin work together to store iron.	ABSTRACT
+44	56	encapsulated	protein_state	It is also not clear how encapsulin and the encapsulated ferritin work together to store iron.	ABSTRACT
+57	65	ferritin	protein_type	It is also not clear how encapsulin and the encapsulated ferritin work together to store iron.	ABSTRACT
+89	93	iron	chemical	It is also not clear how encapsulin and the encapsulated ferritin work together to store iron.	ABSTRACT
+42	63	X-ray crystallography	experimental_method	He et al. have now used the techniques of X-ray crystallography and mass spectrometry to determine the structure of the encapsulated ferritin found in some bacteria.	ABSTRACT
+68	85	mass spectrometry	experimental_method	He et al. have now used the techniques of X-ray crystallography and mass spectrometry to determine the structure of the encapsulated ferritin found in some bacteria.	ABSTRACT
+103	112	structure	evidence	He et al. have now used the techniques of X-ray crystallography and mass spectrometry to determine the structure of the encapsulated ferritin found in some bacteria.	ABSTRACT
+120	132	encapsulated	protein_state	He et al. have now used the techniques of X-ray crystallography and mass spectrometry to determine the structure of the encapsulated ferritin found in some bacteria.	ABSTRACT
+133	141	ferritin	protein_type	He et al. have now used the techniques of X-ray crystallography and mass spectrometry to determine the structure of the encapsulated ferritin found in some bacteria.	ABSTRACT
+156	164	bacteria	taxonomy_domain	He et al. have now used the techniques of X-ray crystallography and mass spectrometry to determine the structure of the encapsulated ferritin found in some bacteria.	ABSTRACT
+4	16	encapsulated	protein_state	The encapsulated ferritin forms a ring-shaped doughnut in which ten subunits of ferritin are arranged in a ring; this is totally different from the enclosed cages that other ferritins form.	ABSTRACT
+17	25	ferritin	protein_type	The encapsulated ferritin forms a ring-shaped doughnut in which ten subunits of ferritin are arranged in a ring; this is totally different from the enclosed cages that other ferritins form.	ABSTRACT
+34	45	ring-shaped	structure_element	The encapsulated ferritin forms a ring-shaped doughnut in which ten subunits of ferritin are arranged in a ring; this is totally different from the enclosed cages that other ferritins form.	ABSTRACT
+46	54	doughnut	structure_element	The encapsulated ferritin forms a ring-shaped doughnut in which ten subunits of ferritin are arranged in a ring; this is totally different from the enclosed cages that other ferritins form.	ABSTRACT
+68	76	subunits	structure_element	The encapsulated ferritin forms a ring-shaped doughnut in which ten subunits of ferritin are arranged in a ring; this is totally different from the enclosed cages that other ferritins form.	ABSTRACT
+80	88	ferritin	protein_type	The encapsulated ferritin forms a ring-shaped doughnut in which ten subunits of ferritin are arranged in a ring; this is totally different from the enclosed cages that other ferritins form.	ABSTRACT
+107	111	ring	structure_element	The encapsulated ferritin forms a ring-shaped doughnut in which ten subunits of ferritin are arranged in a ring; this is totally different from the enclosed cages that other ferritins form.	ABSTRACT
+157	162	cages	structure_element	The encapsulated ferritin forms a ring-shaped doughnut in which ten subunits of ferritin are arranged in a ring; this is totally different from the enclosed cages that other ferritins form.	ABSTRACT
+174	183	ferritins	protein_type	The encapsulated ferritin forms a ring-shaped doughnut in which ten subunits of ferritin are arranged in a ring; this is totally different from the enclosed cages that other ferritins form.	ABSTRACT
+0	19	Biochemical studies	experimental_method	Biochemical studies revealed that the encapsulated ferritin is able to convert iron into a less reactive form, but it cannot store iron on its own since it does not form a cage.	ABSTRACT
+38	50	encapsulated	protein_state	Biochemical studies revealed that the encapsulated ferritin is able to convert iron into a less reactive form, but it cannot store iron on its own since it does not form a cage.	ABSTRACT
+51	59	ferritin	protein_type	Biochemical studies revealed that the encapsulated ferritin is able to convert iron into a less reactive form, but it cannot store iron on its own since it does not form a cage.	ABSTRACT
+79	83	iron	chemical	Biochemical studies revealed that the encapsulated ferritin is able to convert iron into a less reactive form, but it cannot store iron on its own since it does not form a cage.	ABSTRACT
+131	135	iron	chemical	Biochemical studies revealed that the encapsulated ferritin is able to convert iron into a less reactive form, but it cannot store iron on its own since it does not form a cage.	ABSTRACT
+10	22	encapsulated	protein_state	Thus, the encapsulated ferritin needs to be housed within the encapsulin cage to store iron.	ABSTRACT
+23	31	ferritin	protein_type	Thus, the encapsulated ferritin needs to be housed within the encapsulin cage to store iron.	ABSTRACT
+62	72	encapsulin	protein	Thus, the encapsulated ferritin needs to be housed within the encapsulin cage to store iron.	ABSTRACT
+87	91	iron	chemical	Thus, the encapsulated ferritin needs to be housed within the encapsulin cage to store iron.	ABSTRACT
+42	46	iron	chemical	Further work is needed to investigate how iron moves into the encapsulin cage to reach the ferritin proteins.	ABSTRACT
+62	72	encapsulin	protein	Further work is needed to investigate how iron moves into the encapsulin cage to reach the ferritin proteins.	ABSTRACT
+91	99	ferritin	protein_type	Further work is needed to investigate how iron moves into the encapsulin cage to reach the ferritin proteins.	ABSTRACT
+34	42	ferritin	protein_type	Some organisms have both standard ferritin cages and encapsulated ferritins; why this is the case also remains to be discovered.	ABSTRACT
+53	65	encapsulated	protein_state	Some organisms have both standard ferritin cages and encapsulated ferritins; why this is the case also remains to be discovered.	ABSTRACT
+66	75	ferritins	protein_type	Some organisms have both standard ferritin cages and encapsulated ferritins; why this is the case also remains to be discovered.	ABSTRACT
+0	10	Encapsulin	protein_type	Encapsulin nanocompartments are a family of proteinaceous metabolic compartments that are widely distributed in bacteria and archaea.	INTRO
+11	27	nanocompartments	complex_assembly	Encapsulin nanocompartments are a family of proteinaceous metabolic compartments that are widely distributed in bacteria and archaea.	INTRO
+112	120	bacteria	taxonomy_domain	Encapsulin nanocompartments are a family of proteinaceous metabolic compartments that are widely distributed in bacteria and archaea.	INTRO
+125	132	archaea	taxonomy_domain	Encapsulin nanocompartments are a family of proteinaceous metabolic compartments that are widely distributed in bacteria and archaea.	INTRO
+48	59	icosahedral	protein_state	They share a common architecture, comprising an icosahedral shell formed by the oligomeric assembly of a protein, encapsulin, that is structurally related to the HK97 bacteriophage capsid protein gp5.	INTRO
+60	65	shell	structure_element	They share a common architecture, comprising an icosahedral shell formed by the oligomeric assembly of a protein, encapsulin, that is structurally related to the HK97 bacteriophage capsid protein gp5.	INTRO
+114	124	encapsulin	protein_type	They share a common architecture, comprising an icosahedral shell formed by the oligomeric assembly of a protein, encapsulin, that is structurally related to the HK97 bacteriophage capsid protein gp5.	INTRO
+162	180	HK97 bacteriophage	taxonomy_domain	They share a common architecture, comprising an icosahedral shell formed by the oligomeric assembly of a protein, encapsulin, that is structurally related to the HK97 bacteriophage capsid protein gp5.	INTRO
+196	199	gp5	protein	They share a common architecture, comprising an icosahedral shell formed by the oligomeric assembly of a protein, encapsulin, that is structurally related to the HK97 bacteriophage capsid protein gp5.	INTRO
+0	3	Gp5	protein	Gp5 is known to assemble as a 66 nm diameter icosahedral shell of 420 subunits.	INTRO
+45	56	icosahedral	protein_state	Gp5 is known to assemble as a 66 nm diameter icosahedral shell of 420 subunits.	INTRO
+57	62	shell	structure_element	Gp5 is known to assemble as a 66 nm diameter icosahedral shell of 420 subunits.	INTRO
+70	78	subunits	structure_element	Gp5 is known to assemble as a 66 nm diameter icosahedral shell of 420 subunits.	INTRO
+22	41	Pyrococcus furiosus	species	In contrast, both the Pyrococcus furiosus and Myxococcus xanthus encapsulin shell-proteins form 32 nm icosahedra with 180 subunits; while the Thermotoga maritima encapsulin is smaller still with a 25 nm, 60-subunit icosahedron.	INTRO
+46	64	Myxococcus xanthus	species	In contrast, both the Pyrococcus furiosus and Myxococcus xanthus encapsulin shell-proteins form 32 nm icosahedra with 180 subunits; while the Thermotoga maritima encapsulin is smaller still with a 25 nm, 60-subunit icosahedron.	INTRO
+65	75	encapsulin	protein	In contrast, both the Pyrococcus furiosus and Myxococcus xanthus encapsulin shell-proteins form 32 nm icosahedra with 180 subunits; while the Thermotoga maritima encapsulin is smaller still with a 25 nm, 60-subunit icosahedron.	INTRO
+76	81	shell	structure_element	In contrast, both the Pyrococcus furiosus and Myxococcus xanthus encapsulin shell-proteins form 32 nm icosahedra with 180 subunits; while the Thermotoga maritima encapsulin is smaller still with a 25 nm, 60-subunit icosahedron.	INTRO
+102	112	icosahedra	structure_element	In contrast, both the Pyrococcus furiosus and Myxococcus xanthus encapsulin shell-proteins form 32 nm icosahedra with 180 subunits; while the Thermotoga maritima encapsulin is smaller still with a 25 nm, 60-subunit icosahedron.	INTRO
+122	130	subunits	structure_element	In contrast, both the Pyrococcus furiosus and Myxococcus xanthus encapsulin shell-proteins form 32 nm icosahedra with 180 subunits; while the Thermotoga maritima encapsulin is smaller still with a 25 nm, 60-subunit icosahedron.	INTRO
+142	161	Thermotoga maritima	species	In contrast, both the Pyrococcus furiosus and Myxococcus xanthus encapsulin shell-proteins form 32 nm icosahedra with 180 subunits; while the Thermotoga maritima encapsulin is smaller still with a 25 nm, 60-subunit icosahedron.	INTRO
+162	172	encapsulin	protein	In contrast, both the Pyrococcus furiosus and Myxococcus xanthus encapsulin shell-proteins form 32 nm icosahedra with 180 subunits; while the Thermotoga maritima encapsulin is smaller still with a 25 nm, 60-subunit icosahedron.	INTRO
+215	226	icosahedron	structure_element	In contrast, both the Pyrococcus furiosus and Myxococcus xanthus encapsulin shell-proteins form 32 nm icosahedra with 180 subunits; while the Thermotoga maritima encapsulin is smaller still with a 25 nm, 60-subunit icosahedron.	INTRO
+38	48	encapsulin	protein_type	The high structural similarity of the encapsulin shell-proteins to gp5 suggests a common evolutionary origin for these proteins.	INTRO
+49	54	shell	structure_element	The high structural similarity of the encapsulin shell-proteins to gp5 suggests a common evolutionary origin for these proteins.	INTRO
+67	70	gp5	protein	The high structural similarity of the encapsulin shell-proteins to gp5 suggests a common evolutionary origin for these proteins.	INTRO
+19	29	encapsulin	protein_type	The genes encoding encapsulin proteins are found downstream of genes for dye-dependent peroxidase (DyP) family enzymes, or encapsulin-associated ferritins (EncFtn).	INTRO
+73	97	dye-dependent peroxidase	protein_type	The genes encoding encapsulin proteins are found downstream of genes for dye-dependent peroxidase (DyP) family enzymes, or encapsulin-associated ferritins (EncFtn).	INTRO
+99	102	DyP	protein_type	The genes encoding encapsulin proteins are found downstream of genes for dye-dependent peroxidase (DyP) family enzymes, or encapsulin-associated ferritins (EncFtn).	INTRO
+123	154	encapsulin-associated ferritins	protein_type	The genes encoding encapsulin proteins are found downstream of genes for dye-dependent peroxidase (DyP) family enzymes, or encapsulin-associated ferritins (EncFtn).	INTRO
+156	162	EncFtn	protein_type	The genes encoding encapsulin proteins are found downstream of genes for dye-dependent peroxidase (DyP) family enzymes, or encapsulin-associated ferritins (EncFtn).	INTRO
+15	25	DyP family	protein_type	Enzymes in the DyP family are active against polyphenolic compounds such as azo dyes and lignin breakdown products; although their physiological function and natural substrates are not known.	INTRO
+0	8	Ferritin	protein_type	Ferritin family proteins are found in all kingdoms and have a wide range of activities, including ribonucleotide reductase, protecting DNA from oxidative damage, and iron storage.	INTRO
+42	50	kingdoms	taxonomy_domain	Ferritin family proteins are found in all kingdoms and have a wide range of activities, including ribonucleotide reductase, protecting DNA from oxidative damage, and iron storage.	INTRO
+98	122	ribonucleotide reductase	protein_type	Ferritin family proteins are found in all kingdoms and have a wide range of activities, including ribonucleotide reductase, protecting DNA from oxidative damage, and iron storage.	INTRO
+166	170	iron	chemical	Ferritin family proteins are found in all kingdoms and have a wide range of activities, including ribonucleotide reductase, protecting DNA from oxidative damage, and iron storage.	INTRO
+4	13	classical	protein_state	The classical iron storage ferritin nanocages are found in all kingdoms and are essential in eukaryotes; they play a central role in iron homeostasis, where they protect the cell from toxic free Fe2+ by oxidizing it and storing the resulting Fe3+ as ferrihydrite minerals within their central cavity.	INTRO
+14	45	iron storage ferritin nanocages	complex_assembly	The classical iron storage ferritin nanocages are found in all kingdoms and are essential in eukaryotes; they play a central role in iron homeostasis, where they protect the cell from toxic free Fe2+ by oxidizing it and storing the resulting Fe3+ as ferrihydrite minerals within their central cavity.	INTRO
+63	71	kingdoms	taxonomy_domain	The classical iron storage ferritin nanocages are found in all kingdoms and are essential in eukaryotes; they play a central role in iron homeostasis, where they protect the cell from toxic free Fe2+ by oxidizing it and storing the resulting Fe3+ as ferrihydrite minerals within their central cavity.	INTRO
+93	103	eukaryotes	taxonomy_domain	The classical iron storage ferritin nanocages are found in all kingdoms and are essential in eukaryotes; they play a central role in iron homeostasis, where they protect the cell from toxic free Fe2+ by oxidizing it and storing the resulting Fe3+ as ferrihydrite minerals within their central cavity.	INTRO
+133	137	iron	chemical	The classical iron storage ferritin nanocages are found in all kingdoms and are essential in eukaryotes; they play a central role in iron homeostasis, where they protect the cell from toxic free Fe2+ by oxidizing it and storing the resulting Fe3+ as ferrihydrite minerals within their central cavity.	INTRO
+195	199	Fe2+	chemical	The classical iron storage ferritin nanocages are found in all kingdoms and are essential in eukaryotes; they play a central role in iron homeostasis, where they protect the cell from toxic free Fe2+ by oxidizing it and storing the resulting Fe3+ as ferrihydrite minerals within their central cavity.	INTRO
+242	246	Fe3+	chemical	The classical iron storage ferritin nanocages are found in all kingdoms and are essential in eukaryotes; they play a central role in iron homeostasis, where they protect the cell from toxic free Fe2+ by oxidizing it and storing the resulting Fe3+ as ferrihydrite minerals within their central cavity.	INTRO
+250	262	ferrihydrite	chemical	The classical iron storage ferritin nanocages are found in all kingdoms and are essential in eukaryotes; they play a central role in iron homeostasis, where they protect the cell from toxic free Fe2+ by oxidizing it and storing the resulting Fe3+ as ferrihydrite minerals within their central cavity.	INTRO
+285	299	central cavity	site	The classical iron storage ferritin nanocages are found in all kingdoms and are essential in eukaryotes; they play a central role in iron homeostasis, where they protect the cell from toxic free Fe2+ by oxidizing it and storing the resulting Fe3+ as ferrihydrite minerals within their central cavity.	INTRO
+4	14	encapsulin	protein_type	The encapsulin-associated enzymes are sequestered within the icosahedral shell through interactions between the shell’s inner surface and a short localization sequence (Gly-Ser-Leu-Lys) appended to their C-termini.	INTRO
+61	72	icosahedral	protein_state	The encapsulin-associated enzymes are sequestered within the icosahedral shell through interactions between the shell’s inner surface and a short localization sequence (Gly-Ser-Leu-Lys) appended to their C-termini.	INTRO
+73	78	shell	structure_element	The encapsulin-associated enzymes are sequestered within the icosahedral shell through interactions between the shell’s inner surface and a short localization sequence (Gly-Ser-Leu-Lys) appended to their C-termini.	INTRO
+112	117	shell	structure_element	The encapsulin-associated enzymes are sequestered within the icosahedral shell through interactions between the shell’s inner surface and a short localization sequence (Gly-Ser-Leu-Lys) appended to their C-termini.	INTRO
+140	167	short localization sequence	structure_element	The encapsulin-associated enzymes are sequestered within the icosahedral shell through interactions between the shell’s inner surface and a short localization sequence (Gly-Ser-Leu-Lys) appended to their C-termini.	INTRO
+169	184	Gly-Ser-Leu-Lys	structure_element	The encapsulin-associated enzymes are sequestered within the icosahedral shell through interactions between the shell’s inner surface and a short localization sequence (Gly-Ser-Leu-Lys) appended to their C-termini.	INTRO
+0	10	This motif	structure_element	This motif is well-conserved, and the addition of this sequence to heterologous proteins is sufficient to direct them to the interior of encapsulins.	INTRO
+14	28	well-conserved	protein_state	This motif is well-conserved, and the addition of this sequence to heterologous proteins is sufficient to direct them to the interior of encapsulins.	INTRO
+137	148	encapsulins	protein_type	This motif is well-conserved, and the addition of this sequence to heterologous proteins is sufficient to direct them to the interior of encapsulins.	INTRO
+22	40	Myxococcus xanthus	species	A recent study of the Myxococcus xanthus encapsulin showed that it sequesters a number of different EncFtn proteins and acts as an ‘iron-megastore’ to protect these bacteria from oxidative stress.	INTRO
+41	51	encapsulin	protein	A recent study of the Myxococcus xanthus encapsulin showed that it sequesters a number of different EncFtn proteins and acts as an ‘iron-megastore’ to protect these bacteria from oxidative stress.	INTRO
+100	106	EncFtn	protein_type	A recent study of the Myxococcus xanthus encapsulin showed that it sequesters a number of different EncFtn proteins and acts as an ‘iron-megastore’ to protect these bacteria from oxidative stress.	INTRO
+132	136	iron	chemical	A recent study of the Myxococcus xanthus encapsulin showed that it sequesters a number of different EncFtn proteins and acts as an ‘iron-megastore’ to protect these bacteria from oxidative stress.	INTRO
+165	173	bacteria	taxonomy_domain	A recent study of the Myxococcus xanthus encapsulin showed that it sequesters a number of different EncFtn proteins and acts as an ‘iron-megastore’ to protect these bacteria from oxidative stress.	INTRO
+66	74	ferritin	protein_type	At 32 nm in diameter, it is much larger than other members of the ferritin superfamily, such as the 12 nm 24-subunit classical ferritin nanocage and the 8 nm 12-subunit Dps (DNA-binding protein from starved cells) complex; and is thus capable of sequestering up to ten times more iron than these ferritins.	INTRO
+117	126	classical	protein_state	At 32 nm in diameter, it is much larger than other members of the ferritin superfamily, such as the 12 nm 24-subunit classical ferritin nanocage and the 8 nm 12-subunit Dps (DNA-binding protein from starved cells) complex; and is thus capable of sequestering up to ten times more iron than these ferritins.	INTRO
+127	135	ferritin	protein_type	At 32 nm in diameter, it is much larger than other members of the ferritin superfamily, such as the 12 nm 24-subunit classical ferritin nanocage and the 8 nm 12-subunit Dps (DNA-binding protein from starved cells) complex; and is thus capable of sequestering up to ten times more iron than these ferritins.	INTRO
+136	144	nanocage	complex_assembly	At 32 nm in diameter, it is much larger than other members of the ferritin superfamily, such as the 12 nm 24-subunit classical ferritin nanocage and the 8 nm 12-subunit Dps (DNA-binding protein from starved cells) complex; and is thus capable of sequestering up to ten times more iron than these ferritins.	INTRO
+169	172	Dps	protein_type	At 32 nm in diameter, it is much larger than other members of the ferritin superfamily, such as the 12 nm 24-subunit classical ferritin nanocage and the 8 nm 12-subunit Dps (DNA-binding protein from starved cells) complex; and is thus capable of sequestering up to ten times more iron than these ferritins.	INTRO
+174	193	DNA-binding protein	protein_type	At 32 nm in diameter, it is much larger than other members of the ferritin superfamily, such as the 12 nm 24-subunit classical ferritin nanocage and the 8 nm 12-subunit Dps (DNA-binding protein from starved cells) complex; and is thus capable of sequestering up to ten times more iron than these ferritins.	INTRO
+280	284	iron	chemical	At 32 nm in diameter, it is much larger than other members of the ferritin superfamily, such as the 12 nm 24-subunit classical ferritin nanocage and the 8 nm 12-subunit Dps (DNA-binding protein from starved cells) complex; and is thus capable of sequestering up to ten times more iron than these ferritins.	INTRO
+296	305	ferritins	protein_type	At 32 nm in diameter, it is much larger than other members of the ferritin superfamily, such as the 12 nm 24-subunit classical ferritin nanocage and the 8 nm 12-subunit Dps (DNA-binding protein from starved cells) complex; and is thus capable of sequestering up to ten times more iron than these ferritins.	INTRO
+25	31	EncFtn	protein_type	The primary sequences of EncFtn proteins have Glu-X-X-His metal coordination sites, which are shared features of the ferritin family proteins.	INTRO
+46	57	Glu-X-X-His	structure_element	The primary sequences of EncFtn proteins have Glu-X-X-His metal coordination sites, which are shared features of the ferritin family proteins.	INTRO
+58	82	metal coordination sites	site	The primary sequences of EncFtn proteins have Glu-X-X-His metal coordination sites, which are shared features of the ferritin family proteins.	INTRO
+117	125	ferritin	protein_type	The primary sequences of EncFtn proteins have Glu-X-X-His metal coordination sites, which are shared features of the ferritin family proteins.	INTRO
+0	30	Secondary structure prediction	experimental_method	Secondary structure prediction identifies two major α-helical regions in these proteins; this is in contrast to other members of the ferritin superfamily, which have four major α-helices (Supplementary file 1).	INTRO
+46	69	major α-helical regions	structure_element	Secondary structure prediction identifies two major α-helical regions in these proteins; this is in contrast to other members of the ferritin superfamily, which have four major α-helices (Supplementary file 1).	INTRO
+133	141	ferritin	protein_type	Secondary structure prediction identifies two major α-helical regions in these proteins; this is in contrast to other members of the ferritin superfamily, which have four major α-helices (Supplementary file 1).	INTRO
+171	186	major α-helices	structure_element	Secondary structure prediction identifies two major α-helical regions in these proteins; this is in contrast to other members of the ferritin superfamily, which have four major α-helices (Supplementary file 1).	INTRO
+10	18	ferritin	protein_type	The ‘half-ferritin’ primary sequence of the EncFtn family and their association with encapsulin nanocompartments suggests a distinct biochemical and structural organization to other ferritin family proteins.	INTRO
+44	50	EncFtn	protein_type	The ‘half-ferritin’ primary sequence of the EncFtn family and their association with encapsulin nanocompartments suggests a distinct biochemical and structural organization to other ferritin family proteins.	INTRO
+85	95	encapsulin	protein	The ‘half-ferritin’ primary sequence of the EncFtn family and their association with encapsulin nanocompartments suggests a distinct biochemical and structural organization to other ferritin family proteins.	INTRO
+96	112	nanocompartments	complex_assembly	The ‘half-ferritin’ primary sequence of the EncFtn family and their association with encapsulin nanocompartments suggests a distinct biochemical and structural organization to other ferritin family proteins.	INTRO
+182	190	ferritin	protein_type	The ‘half-ferritin’ primary sequence of the EncFtn family and their association with encapsulin nanocompartments suggests a distinct biochemical and structural organization to other ferritin family proteins.	INTRO
+4	25	Rhodospirillum rubrum	species	The Rhodospirillum rubrum EncFtn protein (Rru_A0973) shares 33% protein sequence identity with the M. xanthus (MXAN_4464), 53% with the T. maritima (Tmari_0787), and 29% with the P. furiosus (PF1192) homologues.	INTRO
+26	32	EncFtn	protein	The Rhodospirillum rubrum EncFtn protein (Rru_A0973) shares 33% protein sequence identity with the M. xanthus (MXAN_4464), 53% with the T. maritima (Tmari_0787), and 29% with the P. furiosus (PF1192) homologues.	INTRO
+42	51	Rru_A0973	gene	The Rhodospirillum rubrum EncFtn protein (Rru_A0973) shares 33% protein sequence identity with the M. xanthus (MXAN_4464), 53% with the T. maritima (Tmari_0787), and 29% with the P. furiosus (PF1192) homologues.	INTRO
+99	109	M. xanthus	species	The Rhodospirillum rubrum EncFtn protein (Rru_A0973) shares 33% protein sequence identity with the M. xanthus (MXAN_4464), 53% with the T. maritima (Tmari_0787), and 29% with the P. furiosus (PF1192) homologues.	INTRO
+111	120	MXAN_4464	gene	The Rhodospirillum rubrum EncFtn protein (Rru_A0973) shares 33% protein sequence identity with the M. xanthus (MXAN_4464), 53% with the T. maritima (Tmari_0787), and 29% with the P. furiosus (PF1192) homologues.	INTRO
+136	147	T. maritima	species	The Rhodospirillum rubrum EncFtn protein (Rru_A0973) shares 33% protein sequence identity with the M. xanthus (MXAN_4464), 53% with the T. maritima (Tmari_0787), and 29% with the P. furiosus (PF1192) homologues.	INTRO
+149	159	Tmari_0787	gene	The Rhodospirillum rubrum EncFtn protein (Rru_A0973) shares 33% protein sequence identity with the M. xanthus (MXAN_4464), 53% with the T. maritima (Tmari_0787), and 29% with the P. furiosus (PF1192) homologues.	INTRO
+179	190	P. furiosus	species	The Rhodospirillum rubrum EncFtn protein (Rru_A0973) shares 33% protein sequence identity with the M. xanthus (MXAN_4464), 53% with the T. maritima (Tmari_0787), and 29% with the P. furiosus (PF1192) homologues.	INTRO
+192	198	PF1192	gene	The Rhodospirillum rubrum EncFtn protein (Rru_A0973) shares 33% protein sequence identity with the M. xanthus (MXAN_4464), 53% with the T. maritima (Tmari_0787), and 29% with the P. furiosus (PF1192) homologues.	INTRO
+4	8	GXXH	structure_element	The GXXH motifs are strictly conserved in each of these species (Supplementary file 1).	INTRO
+20	38	strictly conserved	protein_state	The GXXH motifs are strictly conserved in each of these species (Supplementary file 1).	INTRO
+24	33	structure	evidence	Here we investigate the structure and biochemistry of EncFtn in order to understand iron storage within the encapsulin nanocompartment.	INTRO
+54	60	EncFtn	protein	Here we investigate the structure and biochemistry of EncFtn in order to understand iron storage within the encapsulin nanocompartment.	INTRO
+84	88	iron	chemical	Here we investigate the structure and biochemistry of EncFtn in order to understand iron storage within the encapsulin nanocompartment.	INTRO
+108	118	encapsulin	protein	Here we investigate the structure and biochemistry of EncFtn in order to understand iron storage within the encapsulin nanocompartment.	INTRO
+119	134	nanocompartment	complex_assembly	Here we investigate the structure and biochemistry of EncFtn in order to understand iron storage within the encapsulin nanocompartment.	INTRO
+29	39	encapsulin	protein	We have produced recombinant encapsulin (Enc) and EncFtn from the aquatic purple-sulfur bacterium R. rubrum, which serves as a model organism for the study of the control of the bacterial nitrogen fixation machinery, in Escherichia coli.	INTRO
+41	44	Enc	protein	We have produced recombinant encapsulin (Enc) and EncFtn from the aquatic purple-sulfur bacterium R. rubrum, which serves as a model organism for the study of the control of the bacterial nitrogen fixation machinery, in Escherichia coli.	INTRO
+50	56	EncFtn	protein	We have produced recombinant encapsulin (Enc) and EncFtn from the aquatic purple-sulfur bacterium R. rubrum, which serves as a model organism for the study of the control of the bacterial nitrogen fixation machinery, in Escherichia coli.	INTRO
+66	73	aquatic	taxonomy_domain	We have produced recombinant encapsulin (Enc) and EncFtn from the aquatic purple-sulfur bacterium R. rubrum, which serves as a model organism for the study of the control of the bacterial nitrogen fixation machinery, in Escherichia coli.	INTRO
+74	97	purple-sulfur bacterium	taxonomy_domain	We have produced recombinant encapsulin (Enc) and EncFtn from the aquatic purple-sulfur bacterium R. rubrum, which serves as a model organism for the study of the control of the bacterial nitrogen fixation machinery, in Escherichia coli.	INTRO
+98	107	R. rubrum	species	We have produced recombinant encapsulin (Enc) and EncFtn from the aquatic purple-sulfur bacterium R. rubrum, which serves as a model organism for the study of the control of the bacterial nitrogen fixation machinery, in Escherichia coli.	INTRO
+178	187	bacterial	taxonomy_domain	We have produced recombinant encapsulin (Enc) and EncFtn from the aquatic purple-sulfur bacterium R. rubrum, which serves as a model organism for the study of the control of the bacterial nitrogen fixation machinery, in Escherichia coli.	INTRO
+220	236	Escherichia coli	species	We have produced recombinant encapsulin (Enc) and EncFtn from the aquatic purple-sulfur bacterium R. rubrum, which serves as a model organism for the study of the control of the bacterial nitrogen fixation machinery, in Escherichia coli.	INTRO
+12	44	transmission electron microscopy	experimental_method	Analysis by transmission electron microscopy (TEM) indicates that their co-expression leads to the production of an icosahedral nanocompartment with encapsulated EncFtn.	INTRO
+46	49	TEM	experimental_method	Analysis by transmission electron microscopy (TEM) indicates that their co-expression leads to the production of an icosahedral nanocompartment with encapsulated EncFtn.	INTRO
+72	85	co-expression	experimental_method	Analysis by transmission electron microscopy (TEM) indicates that their co-expression leads to the production of an icosahedral nanocompartment with encapsulated EncFtn.	INTRO
+116	127	icosahedral	protein_state	Analysis by transmission electron microscopy (TEM) indicates that their co-expression leads to the production of an icosahedral nanocompartment with encapsulated EncFtn.	INTRO
+128	143	nanocompartment	complex_assembly	Analysis by transmission electron microscopy (TEM) indicates that their co-expression leads to the production of an icosahedral nanocompartment with encapsulated EncFtn.	INTRO
+149	161	encapsulated	protein_state	Analysis by transmission electron microscopy (TEM) indicates that their co-expression leads to the production of an icosahedral nanocompartment with encapsulated EncFtn.	INTRO
+162	168	EncFtn	protein	Analysis by transmission electron microscopy (TEM) indicates that their co-expression leads to the production of an icosahedral nanocompartment with encapsulated EncFtn.	INTRO
+4	21	crystal structure	evidence	The crystal structure of a truncated hexahistidine-tagged variant of the EncFtn protein (EncFtnsH) shows that it forms a decameric structure with an annular ‘ring-doughnut’ topology, which is distinct from the four-helical bundles of the 24meric ferritins and dodecahedral DPS proteins.	INTRO
+27	36	truncated	protein_state	The crystal structure of a truncated hexahistidine-tagged variant of the EncFtn protein (EncFtnsH) shows that it forms a decameric structure with an annular ‘ring-doughnut’ topology, which is distinct from the four-helical bundles of the 24meric ferritins and dodecahedral DPS proteins.	INTRO
+37	57	hexahistidine-tagged	protein_state	The crystal structure of a truncated hexahistidine-tagged variant of the EncFtn protein (EncFtnsH) shows that it forms a decameric structure with an annular ‘ring-doughnut’ topology, which is distinct from the four-helical bundles of the 24meric ferritins and dodecahedral DPS proteins.	INTRO
+73	79	EncFtn	protein	The crystal structure of a truncated hexahistidine-tagged variant of the EncFtn protein (EncFtnsH) shows that it forms a decameric structure with an annular ‘ring-doughnut’ topology, which is distinct from the four-helical bundles of the 24meric ferritins and dodecahedral DPS proteins.	INTRO
+89	97	EncFtnsH	protein	The crystal structure of a truncated hexahistidine-tagged variant of the EncFtn protein (EncFtnsH) shows that it forms a decameric structure with an annular ‘ring-doughnut’ topology, which is distinct from the four-helical bundles of the 24meric ferritins and dodecahedral DPS proteins.	INTRO
+121	130	decameric	oligomeric_state	The crystal structure of a truncated hexahistidine-tagged variant of the EncFtn protein (EncFtnsH) shows that it forms a decameric structure with an annular ‘ring-doughnut’ topology, which is distinct from the four-helical bundles of the 24meric ferritins and dodecahedral DPS proteins.	INTRO
+131	140	structure	evidence	The crystal structure of a truncated hexahistidine-tagged variant of the EncFtn protein (EncFtnsH) shows that it forms a decameric structure with an annular ‘ring-doughnut’ topology, which is distinct from the four-helical bundles of the 24meric ferritins and dodecahedral DPS proteins.	INTRO
+158	171	ring-doughnut	structure_element	The crystal structure of a truncated hexahistidine-tagged variant of the EncFtn protein (EncFtnsH) shows that it forms a decameric structure with an annular ‘ring-doughnut’ topology, which is distinct from the four-helical bundles of the 24meric ferritins and dodecahedral DPS proteins.	INTRO
+210	230	four-helical bundles	structure_element	The crystal structure of a truncated hexahistidine-tagged variant of the EncFtn protein (EncFtnsH) shows that it forms a decameric structure with an annular ‘ring-doughnut’ topology, which is distinct from the four-helical bundles of the 24meric ferritins and dodecahedral DPS proteins.	INTRO
+238	245	24meric	oligomeric_state	The crystal structure of a truncated hexahistidine-tagged variant of the EncFtn protein (EncFtnsH) shows that it forms a decameric structure with an annular ‘ring-doughnut’ topology, which is distinct from the four-helical bundles of the 24meric ferritins and dodecahedral DPS proteins.	INTRO
+246	255	ferritins	protein_type	The crystal structure of a truncated hexahistidine-tagged variant of the EncFtn protein (EncFtnsH) shows that it forms a decameric structure with an annular ‘ring-doughnut’ topology, which is distinct from the four-helical bundles of the 24meric ferritins and dodecahedral DPS proteins.	INTRO
+260	272	dodecahedral	oligomeric_state	The crystal structure of a truncated hexahistidine-tagged variant of the EncFtn protein (EncFtnsH) shows that it forms a decameric structure with an annular ‘ring-doughnut’ topology, which is distinct from the four-helical bundles of the 24meric ferritins and dodecahedral DPS proteins.	INTRO
+273	276	DPS	protein_type	The crystal structure of a truncated hexahistidine-tagged variant of the EncFtn protein (EncFtnsH) shows that it forms a decameric structure with an annular ‘ring-doughnut’ topology, which is distinct from the four-helical bundles of the 24meric ferritins and dodecahedral DPS proteins.	INTRO
+26	36	iron bound	protein_state	We identify a symmetrical iron bound ferroxidase center (FOC) formed between subunits in the decamer and additional metal-binding sites close to the center of the ring and on the outer surface.	INTRO
+37	55	ferroxidase center	site	We identify a symmetrical iron bound ferroxidase center (FOC) formed between subunits in the decamer and additional metal-binding sites close to the center of the ring and on the outer surface.	INTRO
+57	60	FOC	site	We identify a symmetrical iron bound ferroxidase center (FOC) formed between subunits in the decamer and additional metal-binding sites close to the center of the ring and on the outer surface.	INTRO
+77	85	subunits	structure_element	We identify a symmetrical iron bound ferroxidase center (FOC) formed between subunits in the decamer and additional metal-binding sites close to the center of the ring and on the outer surface.	INTRO
+93	100	decamer	oligomeric_state	We identify a symmetrical iron bound ferroxidase center (FOC) formed between subunits in the decamer and additional metal-binding sites close to the center of the ring and on the outer surface.	INTRO
+116	135	metal-binding sites	site	We identify a symmetrical iron bound ferroxidase center (FOC) formed between subunits in the decamer and additional metal-binding sites close to the center of the ring and on the outer surface.	INTRO
+163	167	ring	structure_element	We identify a symmetrical iron bound ferroxidase center (FOC) formed between subunits in the decamer and additional metal-binding sites close to the center of the ring and on the outer surface.	INTRO
+52	58	EncFtn	protein	We also demonstrate the metal-dependent assembly of EncFtn decamers using native PAGE, analytical gel-filtration, and native mass spectrometry.	INTRO
+59	67	decamers	oligomeric_state	We also demonstrate the metal-dependent assembly of EncFtn decamers using native PAGE, analytical gel-filtration, and native mass spectrometry.	INTRO
+74	85	native PAGE	experimental_method	We also demonstrate the metal-dependent assembly of EncFtn decamers using native PAGE, analytical gel-filtration, and native mass spectrometry.	INTRO
+87	112	analytical gel-filtration	experimental_method	We also demonstrate the metal-dependent assembly of EncFtn decamers using native PAGE, analytical gel-filtration, and native mass spectrometry.	INTRO
+118	142	native mass spectrometry	experimental_method	We also demonstrate the metal-dependent assembly of EncFtn decamers using native PAGE, analytical gel-filtration, and native mass spectrometry.	INTRO
+0	18	Biochemical assays	experimental_method	Biochemical assays show that EncFtn is active as a ferroxidase enzyme.	INTRO
+29	35	EncFtn	protein	Biochemical assays show that EncFtn is active as a ferroxidase enzyme.	INTRO
+39	45	active	protein_state	Biochemical assays show that EncFtn is active as a ferroxidase enzyme.	INTRO
+51	62	ferroxidase	protein_type	Biochemical assays show that EncFtn is active as a ferroxidase enzyme.	INTRO
+8	33	site-directed mutagenesis	experimental_method	Through site-directed mutagenesis we show that the conserved glutamic acid and histidine residues in the FOC influence protein assembly and activity.	INTRO
+51	60	conserved	protein_state	Through site-directed mutagenesis we show that the conserved glutamic acid and histidine residues in the FOC influence protein assembly and activity.	INTRO
+61	74	glutamic acid	residue_name	Through site-directed mutagenesis we show that the conserved glutamic acid and histidine residues in the FOC influence protein assembly and activity.	INTRO
+79	88	histidine	residue_name	Through site-directed mutagenesis we show that the conserved glutamic acid and histidine residues in the FOC influence protein assembly and activity.	INTRO
+105	108	FOC	site	Through site-directed mutagenesis we show that the conserved glutamic acid and histidine residues in the FOC influence protein assembly and activity.	INTRO
+20	51	structural and biochemical data	evidence	We use our combined structural and biochemical data to propose a model for the EncFtn-catalyzed sequestration of iron within the encapsulin shell.	INTRO
+79	85	EncFtn	protein	We use our combined structural and biochemical data to propose a model for the EncFtn-catalyzed sequestration of iron within the encapsulin shell.	INTRO
+113	117	iron	chemical	We use our combined structural and biochemical data to propose a model for the EncFtn-catalyzed sequestration of iron within the encapsulin shell.	INTRO
+129	139	encapsulin	protein	We use our combined structural and biochemical data to propose a model for the EncFtn-catalyzed sequestration of iron within the encapsulin shell.	INTRO
+140	145	shell	structure_element	We use our combined structural and biochemical data to propose a model for the EncFtn-catalyzed sequestration of iron within the encapsulin shell.	INTRO
+12	21	R. rubrum	species	Assembly of R. rubrum EncFtn encapsulin nanocompartments in E. coli	RESULTS
+22	28	EncFtn	protein	Assembly of R. rubrum EncFtn encapsulin nanocompartments in E. coli	RESULTS
+29	39	encapsulin	protein	Assembly of R. rubrum EncFtn encapsulin nanocompartments in E. coli	RESULTS
+40	56	nanocompartments	complex_assembly	Assembly of R. rubrum EncFtn encapsulin nanocompartments in E. coli	RESULTS
+60	67	E. coli	species	Assembly of R. rubrum EncFtn encapsulin nanocompartments in E. coli	RESULTS
+0	44	Full-frame transmission electron micrographs	evidence	Full-frame transmission electron micrographs of R. rubrum nanocompartments.	FIG
+48	57	R. rubrum	species	Full-frame transmission electron micrographs of R. rubrum nanocompartments.	FIG
+58	74	nanocompartments	complex_assembly	Full-frame transmission electron micrographs of R. rubrum nanocompartments.	FIG
+6	24	Negative stain TEM	experimental_method	(A/B) Negative stain TEM image of recombinant R. rubrum encapsulin and EncFtn-Enc nanocompartments.	FIG
+25	30	image	evidence	(A/B) Negative stain TEM image of recombinant R. rubrum encapsulin and EncFtn-Enc nanocompartments.	FIG
+46	55	R. rubrum	species	(A/B) Negative stain TEM image of recombinant R. rubrum encapsulin and EncFtn-Enc nanocompartments.	FIG
+56	66	encapsulin	protein	(A/B) Negative stain TEM image of recombinant R. rubrum encapsulin and EncFtn-Enc nanocompartments.	FIG
+71	81	EncFtn-Enc	complex_assembly	(A/B) Negative stain TEM image of recombinant R. rubrum encapsulin and EncFtn-Enc nanocompartments.	FIG
+82	98	nanocompartments	complex_assembly	(A/B) Negative stain TEM image of recombinant R. rubrum encapsulin and EncFtn-Enc nanocompartments.	FIG
+99	108	Histogram	evidence	All samples were imaged at 143,000 x magnification; the scale bar length corresponds to 50 nm. (C) Histogram showing the distribution of nanocompartment diameters.	FIG
+137	152	nanocompartment	complex_assembly	All samples were imaged at 143,000 x magnification; the scale bar length corresponds to 50 nm. (C) Histogram showing the distribution of nanocompartment diameters.	FIG
+8	48	Gaussian nonlinear least square function	experimental_method	A model Gaussian nonlinear least square function was fitted to the data to obtain a mean diameter of 24.6 nm with a standard deviation of 2.0 nm for encapsulin (grey) and a mean value of 23.9 nm with a standard deviation of 2.2 nm for co-expressed EncFtn and encapsulin (EncFtn-Enc, black).	FIG
+149	159	encapsulin	protein	A model Gaussian nonlinear least square function was fitted to the data to obtain a mean diameter of 24.6 nm with a standard deviation of 2.0 nm for encapsulin (grey) and a mean value of 23.9 nm with a standard deviation of 2.2 nm for co-expressed EncFtn and encapsulin (EncFtn-Enc, black).	FIG
+235	247	co-expressed	experimental_method	A model Gaussian nonlinear least square function was fitted to the data to obtain a mean diameter of 24.6 nm with a standard deviation of 2.0 nm for encapsulin (grey) and a mean value of 23.9 nm with a standard deviation of 2.2 nm for co-expressed EncFtn and encapsulin (EncFtn-Enc, black).	FIG
+248	254	EncFtn	protein	A model Gaussian nonlinear least square function was fitted to the data to obtain a mean diameter of 24.6 nm with a standard deviation of 2.0 nm for encapsulin (grey) and a mean value of 23.9 nm with a standard deviation of 2.2 nm for co-expressed EncFtn and encapsulin (EncFtn-Enc, black).	FIG
+259	269	encapsulin	protein	A model Gaussian nonlinear least square function was fitted to the data to obtain a mean diameter of 24.6 nm with a standard deviation of 2.0 nm for encapsulin (grey) and a mean value of 23.9 nm with a standard deviation of 2.2 nm for co-expressed EncFtn and encapsulin (EncFtn-Enc, black).	FIG
+271	281	EncFtn-Enc	complex_assembly	A model Gaussian nonlinear least square function was fitted to the data to obtain a mean diameter of 24.6 nm with a standard deviation of 2.0 nm for encapsulin (grey) and a mean value of 23.9 nm with a standard deviation of 2.2 nm for co-expressed EncFtn and encapsulin (EncFtn-Enc, black).	FIG
+28	37	R. rubrum	species	Purification of recombinant R. rubrum encapsulin nanocompartments.	FIG
+38	48	encapsulin	protein	Purification of recombinant R. rubrum encapsulin nanocompartments.	FIG
+49	65	nanocompartments	complex_assembly	Purification of recombinant R. rubrum encapsulin nanocompartments.	FIG
+4	27	Recombinantly expressed	experimental_method	(A) Recombinantly expressed encapsulin (Enc) and co-expressed EncFtn-Enc were purified by sucrose gradient ultracentrifugation from E. coli B834(DE3) grown in SeMet medium.	FIG
+28	38	encapsulin	protein	(A) Recombinantly expressed encapsulin (Enc) and co-expressed EncFtn-Enc were purified by sucrose gradient ultracentrifugation from E. coli B834(DE3) grown in SeMet medium.	FIG
+40	43	Enc	protein	(A) Recombinantly expressed encapsulin (Enc) and co-expressed EncFtn-Enc were purified by sucrose gradient ultracentrifugation from E. coli B834(DE3) grown in SeMet medium.	FIG
+49	61	co-expressed	experimental_method	(A) Recombinantly expressed encapsulin (Enc) and co-expressed EncFtn-Enc were purified by sucrose gradient ultracentrifugation from E. coli B834(DE3) grown in SeMet medium.	FIG
+62	72	EncFtn-Enc	complex_assembly	(A) Recombinantly expressed encapsulin (Enc) and co-expressed EncFtn-Enc were purified by sucrose gradient ultracentrifugation from E. coli B834(DE3) grown in SeMet medium.	FIG
+90	126	sucrose gradient ultracentrifugation	experimental_method	(A) Recombinantly expressed encapsulin (Enc) and co-expressed EncFtn-Enc were purified by sucrose gradient ultracentrifugation from E. coli B834(DE3) grown in SeMet medium.	FIG
+132	139	E. coli	species	(A) Recombinantly expressed encapsulin (Enc) and co-expressed EncFtn-Enc were purified by sucrose gradient ultracentrifugation from E. coli B834(DE3) grown in SeMet medium.	FIG
+159	164	SeMet	chemical	(A) Recombinantly expressed encapsulin (Enc) and co-expressed EncFtn-Enc were purified by sucrose gradient ultracentrifugation from E. coli B834(DE3) grown in SeMet medium.	FIG
+40	48	SDS-PAGE	experimental_method	Samples were resolved by 18% acrylamide SDS-PAGE; the position of the proteins found in the complexes as resolved on the gel are shown with arrows.	FIG
+6	24	Negative stain TEM	experimental_method	(B/C) Negative stain TEM image of recombinant encapsulin and EncFtn-Enc nanocompartments.	FIG
+46	56	encapsulin	protein	(B/C) Negative stain TEM image of recombinant encapsulin and EncFtn-Enc nanocompartments.	FIG
+61	71	EncFtn-Enc	complex_assembly	(B/C) Negative stain TEM image of recombinant encapsulin and EncFtn-Enc nanocompartments.	FIG
+72	88	nanocompartments	complex_assembly	(B/C) Negative stain TEM image of recombinant encapsulin and EncFtn-Enc nanocompartments.	FIG
+15	25	encapsulin	protein	Representative encapsulin and EncFtn-Enc complexes are indicated with red arrows.	FIG
+30	40	EncFtn-Enc	complex_assembly	Representative encapsulin and EncFtn-Enc complexes are indicated with red arrows.	FIG
+24	33	R. rubrum	species	We produced recombinant R. rubrum encapsulin nanocompartments in E. coli by co-expression of the encapsulin (Rru_A0974) and EncFtn (Rru_A0973) proteins, and purified these by sucrose gradient ultra-centrifugation (Figure 1A).	RESULTS
+34	44	encapsulin	protein	We produced recombinant R. rubrum encapsulin nanocompartments in E. coli by co-expression of the encapsulin (Rru_A0974) and EncFtn (Rru_A0973) proteins, and purified these by sucrose gradient ultra-centrifugation (Figure 1A).	RESULTS
+45	61	nanocompartments	complex_assembly	We produced recombinant R. rubrum encapsulin nanocompartments in E. coli by co-expression of the encapsulin (Rru_A0974) and EncFtn (Rru_A0973) proteins, and purified these by sucrose gradient ultra-centrifugation (Figure 1A).	RESULTS
+65	72	E. coli	species	We produced recombinant R. rubrum encapsulin nanocompartments in E. coli by co-expression of the encapsulin (Rru_A0974) and EncFtn (Rru_A0973) proteins, and purified these by sucrose gradient ultra-centrifugation (Figure 1A).	RESULTS
+76	89	co-expression	experimental_method	We produced recombinant R. rubrum encapsulin nanocompartments in E. coli by co-expression of the encapsulin (Rru_A0974) and EncFtn (Rru_A0973) proteins, and purified these by sucrose gradient ultra-centrifugation (Figure 1A).	RESULTS
+97	107	encapsulin	protein	We produced recombinant R. rubrum encapsulin nanocompartments in E. coli by co-expression of the encapsulin (Rru_A0974) and EncFtn (Rru_A0973) proteins, and purified these by sucrose gradient ultra-centrifugation (Figure 1A).	RESULTS
+109	118	Rru_A0974	gene	We produced recombinant R. rubrum encapsulin nanocompartments in E. coli by co-expression of the encapsulin (Rru_A0974) and EncFtn (Rru_A0973) proteins, and purified these by sucrose gradient ultra-centrifugation (Figure 1A).	RESULTS
+124	130	EncFtn	protein	We produced recombinant R. rubrum encapsulin nanocompartments in E. coli by co-expression of the encapsulin (Rru_A0974) and EncFtn (Rru_A0973) proteins, and purified these by sucrose gradient ultra-centrifugation (Figure 1A).	RESULTS
+132	141	Rru_A0973	gene	We produced recombinant R. rubrum encapsulin nanocompartments in E. coli by co-expression of the encapsulin (Rru_A0974) and EncFtn (Rru_A0973) proteins, and purified these by sucrose gradient ultra-centrifugation (Figure 1A).	RESULTS
+175	212	sucrose gradient ultra-centrifugation	experimental_method	We produced recombinant R. rubrum encapsulin nanocompartments in E. coli by co-expression of the encapsulin (Rru_A0974) and EncFtn (Rru_A0973) proteins, and purified these by sucrose gradient ultra-centrifugation (Figure 1A).	RESULTS
+0	3	TEM	experimental_method	TEM imaging of uranyl acetate-stained samples revealed that, when expressed in isolation, the encapsulin protein forms empty compartments with an average diameter of 24 nm (Figure 1B and Figure 1—figure supplement 1A/C), consistent with the appearance and size of the T. maritima encapsulin.	RESULTS
+66	88	expressed in isolation	experimental_method	TEM imaging of uranyl acetate-stained samples revealed that, when expressed in isolation, the encapsulin protein forms empty compartments with an average diameter of 24 nm (Figure 1B and Figure 1—figure supplement 1A/C), consistent with the appearance and size of the T. maritima encapsulin.	RESULTS
+94	104	encapsulin	protein	TEM imaging of uranyl acetate-stained samples revealed that, when expressed in isolation, the encapsulin protein forms empty compartments with an average diameter of 24 nm (Figure 1B and Figure 1—figure supplement 1A/C), consistent with the appearance and size of the T. maritima encapsulin.	RESULTS
+119	124	empty	protein_state	TEM imaging of uranyl acetate-stained samples revealed that, when expressed in isolation, the encapsulin protein forms empty compartments with an average diameter of 24 nm (Figure 1B and Figure 1—figure supplement 1A/C), consistent with the appearance and size of the T. maritima encapsulin.	RESULTS
+125	137	compartments	complex_assembly	TEM imaging of uranyl acetate-stained samples revealed that, when expressed in isolation, the encapsulin protein forms empty compartments with an average diameter of 24 nm (Figure 1B and Figure 1—figure supplement 1A/C), consistent with the appearance and size of the T. maritima encapsulin.	RESULTS
+268	279	T. maritima	species	TEM imaging of uranyl acetate-stained samples revealed that, when expressed in isolation, the encapsulin protein forms empty compartments with an average diameter of 24 nm (Figure 1B and Figure 1—figure supplement 1A/C), consistent with the appearance and size of the T. maritima encapsulin.	RESULTS
+280	290	encapsulin	protein	TEM imaging of uranyl acetate-stained samples revealed that, when expressed in isolation, the encapsulin protein forms empty compartments with an average diameter of 24 nm (Figure 1B and Figure 1—figure supplement 1A/C), consistent with the appearance and size of the T. maritima encapsulin.	RESULTS
+59	65	EncFtn	protein	We were not able to resolve any higher-order structures of EncFtn by TEM.	RESULTS
+69	72	TEM	experimental_method	We were not able to resolve any higher-order structures of EncFtn by TEM.	RESULTS
+22	35	co-expression	experimental_method	Protein purified from co-expression of the encapsulin and EncFtn resulted in 24 nm compartments with regions in the center that exclude stain, consistent with the presence of the EncFtn within the encapsulin shell (Figure 1C and Figure 1—figure supplement 1B/C).	RESULTS
+43	53	encapsulin	protein	Protein purified from co-expression of the encapsulin and EncFtn resulted in 24 nm compartments with regions in the center that exclude stain, consistent with the presence of the EncFtn within the encapsulin shell (Figure 1C and Figure 1—figure supplement 1B/C).	RESULTS
+58	64	EncFtn	protein	Protein purified from co-expression of the encapsulin and EncFtn resulted in 24 nm compartments with regions in the center that exclude stain, consistent with the presence of the EncFtn within the encapsulin shell (Figure 1C and Figure 1—figure supplement 1B/C).	RESULTS
+163	174	presence of	protein_state	Protein purified from co-expression of the encapsulin and EncFtn resulted in 24 nm compartments with regions in the center that exclude stain, consistent with the presence of the EncFtn within the encapsulin shell (Figure 1C and Figure 1—figure supplement 1B/C).	RESULTS
+179	185	EncFtn	protein	Protein purified from co-expression of the encapsulin and EncFtn resulted in 24 nm compartments with regions in the center that exclude stain, consistent with the presence of the EncFtn within the encapsulin shell (Figure 1C and Figure 1—figure supplement 1B/C).	RESULTS
+197	207	encapsulin	protein	Protein purified from co-expression of the encapsulin and EncFtn resulted in 24 nm compartments with regions in the center that exclude stain, consistent with the presence of the EncFtn within the encapsulin shell (Figure 1C and Figure 1—figure supplement 1B/C).	RESULTS
+208	213	shell	structure_element	Protein purified from co-expression of the encapsulin and EncFtn resulted in 24 nm compartments with regions in the center that exclude stain, consistent with the presence of the EncFtn within the encapsulin shell (Figure 1C and Figure 1—figure supplement 1B/C).	RESULTS
+0	9	R. rubrum	species	R. rubrum EncFtn forms a metal-ion stabilized decamer in solution	RESULTS
+10	16	EncFtn	protein	R. rubrum EncFtn forms a metal-ion stabilized decamer in solution	RESULTS
+46	53	decamer	oligomeric_state	R. rubrum EncFtn forms a metal-ion stabilized decamer in solution	RESULTS
+0	27	Purification of recombinant	experimental_method	Purification of recombinant R. rubrum EncFtnsH.	FIG
+28	37	R. rubrum	species	Purification of recombinant R. rubrum EncFtnsH.	FIG
+38	46	EncFtnsH	protein	Purification of recombinant R. rubrum EncFtnsH.	FIG
+16	29	SeMet-labeled	protein_state	(A) Recombinant SeMet-labeled EncFtnsH produced with 1 mM Fe(NH4)2(SO4)2 in the growth medium was purified by nickel affinity chromatography and size-exclusion chromatography using a Superdex 200 16/60 column (GE Healthcare).	FIG
+30	38	EncFtnsH	protein	(A) Recombinant SeMet-labeled EncFtnsH produced with 1 mM Fe(NH4)2(SO4)2 in the growth medium was purified by nickel affinity chromatography and size-exclusion chromatography using a Superdex 200 16/60 column (GE Healthcare).	FIG
+58	72	Fe(NH4)2(SO4)2	chemical	(A) Recombinant SeMet-labeled EncFtnsH produced with 1 mM Fe(NH4)2(SO4)2 in the growth medium was purified by nickel affinity chromatography and size-exclusion chromatography using a Superdex 200 16/60 column (GE Healthcare).	FIG
+110	140	nickel affinity chromatography	experimental_method	(A) Recombinant SeMet-labeled EncFtnsH produced with 1 mM Fe(NH4)2(SO4)2 in the growth medium was purified by nickel affinity chromatography and size-exclusion chromatography using a Superdex 200 16/60 column (GE Healthcare).	FIG
+145	174	size-exclusion chromatography	experimental_method	(A) Recombinant SeMet-labeled EncFtnsH produced with 1 mM Fe(NH4)2(SO4)2 in the growth medium was purified by nickel affinity chromatography and size-exclusion chromatography using a Superdex 200 16/60 column (GE Healthcare).	FIG
+0	12	Chromatogram	evidence	Chromatogram traces measured at 280 nm and 315 nm are shown with the results from ICP-MS analysis of the iron content of the fractions collected during the experiment.	FIG
+82	88	ICP-MS	experimental_method	Chromatogram traces measured at 280 nm and 315 nm are shown with the results from ICP-MS analysis of the iron content of the fractions collected during the experiment.	FIG
+105	109	iron	chemical	Chromatogram traces measured at 280 nm and 315 nm are shown with the results from ICP-MS analysis of the iron content of the fractions collected during the experiment.	FIG
+39	55	molecular weight	evidence	The peak around 73 ml corresponds to a molecular weight of around 130 kDa when compared to calibration standards; this is consistent with a decamer of EncFtnsH. The small peak at 85 ml corresponds to the 13 kDa monomer compared to the standards.	FIG
+140	147	decamer	oligomeric_state	The peak around 73 ml corresponds to a molecular weight of around 130 kDa when compared to calibration standards; this is consistent with a decamer of EncFtnsH. The small peak at 85 ml corresponds to the 13 kDa monomer compared to the standards.	FIG
+151	159	EncFtnsH	protein	The peak around 73 ml corresponds to a molecular weight of around 130 kDa when compared to calibration standards; this is consistent with a decamer of EncFtnsH. The small peak at 85 ml corresponds to the 13 kDa monomer compared to the standards.	FIG
+211	218	monomer	oligomeric_state	The peak around 73 ml corresponds to a molecular weight of around 130 kDa when compared to calibration standards; this is consistent with a decamer of EncFtnsH. The small peak at 85 ml corresponds to the 13 kDa monomer compared to the standards.	FIG
+9	16	decamer	oligomeric_state	Only the decamer peak contains significant amounts of iron as indicated by the ICP-MS analysis.	FIG
+54	58	iron	chemical	Only the decamer peak contains significant amounts of iron as indicated by the ICP-MS analysis.	FIG
+79	85	ICP-MS	experimental_method	Only the decamer peak contains significant amounts of iron as indicated by the ICP-MS analysis.	FIG
+28	42	gel filtration	experimental_method	(B) Peak fractions from the gel filtration run were resolved by 15% acrylamide SDS-PAGE and stained with Coomassie blue stain.	FIG
+79	87	SDS-PAGE	experimental_method	(B) Peak fractions from the gel filtration run were resolved by 15% acrylamide SDS-PAGE and stained with Coomassie blue stain.	FIG
+49	57	EncFtnsH	protein	The bands around 13 kDa and 26 kDa correspond to EncFtnsH, as identified by MALDI peptide mass fingerprinting.	FIG
+76	109	MALDI peptide mass fingerprinting	experimental_method	The bands around 13 kDa and 26 kDa correspond to EncFtnsH, as identified by MALDI peptide mass fingerprinting.	FIG
+42	49	monomer	oligomeric_state	The band at 13 kDa is consistent with the monomer mass, while the band at 26 kDa is consistent with a dimer of EncFtnsH. The dimer species only appears in the decamer fractions.	FIG
+102	107	dimer	oligomeric_state	The band at 13 kDa is consistent with the monomer mass, while the band at 26 kDa is consistent with a dimer of EncFtnsH. The dimer species only appears in the decamer fractions.	FIG
+111	119	EncFtnsH	protein	The band at 13 kDa is consistent with the monomer mass, while the band at 26 kDa is consistent with a dimer of EncFtnsH. The dimer species only appears in the decamer fractions.	FIG
+125	130	dimer	oligomeric_state	The band at 13 kDa is consistent with the monomer mass, while the band at 26 kDa is consistent with a dimer of EncFtnsH. The dimer species only appears in the decamer fractions.	FIG
+159	166	decamer	oligomeric_state	The band at 13 kDa is consistent with the monomer mass, while the band at 26 kDa is consistent with a dimer of EncFtnsH. The dimer species only appears in the decamer fractions.	FIG
+4	13	SEC-MALLS	experimental_method	(C) SEC-MALLS analysis of EncFtnsH from decamer fractions and monomer fractions allows assignment of an average mass of 132 kDa to decamer fractions and 13 kDa to monomer fractions, consistent with decamer and monomer species (Table 2).	FIG
+26	34	EncFtnsH	protein	(C) SEC-MALLS analysis of EncFtnsH from decamer fractions and monomer fractions allows assignment of an average mass of 132 kDa to decamer fractions and 13 kDa to monomer fractions, consistent with decamer and monomer species (Table 2).	FIG
+40	47	decamer	oligomeric_state	(C) SEC-MALLS analysis of EncFtnsH from decamer fractions and monomer fractions allows assignment of an average mass of 132 kDa to decamer fractions and 13 kDa to monomer fractions, consistent with decamer and monomer species (Table 2).	FIG
+62	69	monomer	oligomeric_state	(C) SEC-MALLS analysis of EncFtnsH from decamer fractions and monomer fractions allows assignment of an average mass of 132 kDa to decamer fractions and 13 kDa to monomer fractions, consistent with decamer and monomer species (Table 2).	FIG
+131	138	decamer	oligomeric_state	(C) SEC-MALLS analysis of EncFtnsH from decamer fractions and monomer fractions allows assignment of an average mass of 132 kDa to decamer fractions and 13 kDa to monomer fractions, consistent with decamer and monomer species (Table 2).	FIG
+163	170	monomer	oligomeric_state	(C) SEC-MALLS analysis of EncFtnsH from decamer fractions and monomer fractions allows assignment of an average mass of 132 kDa to decamer fractions and 13 kDa to monomer fractions, consistent with decamer and monomer species (Table 2).	FIG
+198	205	decamer	oligomeric_state	(C) SEC-MALLS analysis of EncFtnsH from decamer fractions and monomer fractions allows assignment of an average mass of 132 kDa to decamer fractions and 13 kDa to monomer fractions, consistent with decamer and monomer species (Table 2).	FIG
+210	217	monomer	oligomeric_state	(C) SEC-MALLS analysis of EncFtnsH from decamer fractions and monomer fractions allows assignment of an average mass of 132 kDa to decamer fractions and 13 kDa to monomer fractions, consistent with decamer and monomer species (Table 2).	FIG
+21	23	Fe	chemical	Determination of the Fe/EncFtnsH protein ratio by ICP-MS.	TABLE
+24	32	EncFtnsH	protein	Determination of the Fe/EncFtnsH protein ratio by ICP-MS.	TABLE
+50	56	ICP-MS	experimental_method	Determination of the Fe/EncFtnsH protein ratio by ICP-MS.	TABLE
+0	8	EncFtnsH	protein	EncFtnsH was purified as a SeMet derivative from E. coli B834(DE3) cells grown in SeMet medium with 1 mM Fe(NH4)2(SO4)2.	TABLE
+27	32	SeMet	chemical	EncFtnsH was purified as a SeMet derivative from E. coli B834(DE3) cells grown in SeMet medium with 1 mM Fe(NH4)2(SO4)2.	TABLE
+49	66	E. coli B834(DE3)	species	EncFtnsH was purified as a SeMet derivative from E. coli B834(DE3) cells grown in SeMet medium with 1 mM Fe(NH4)2(SO4)2.	TABLE
+82	87	SeMet	chemical	EncFtnsH was purified as a SeMet derivative from E. coli B834(DE3) cells grown in SeMet medium with 1 mM Fe(NH4)2(SO4)2.	TABLE
+105	119	Fe(NH4)2(SO4)2	chemical	EncFtnsH was purified as a SeMet derivative from E. coli B834(DE3) cells grown in SeMet medium with 1 mM Fe(NH4)2(SO4)2.	TABLE
+15	18	SEC	experimental_method	Fractions from SEC were collected, acidified and analysed by ICP-MS.	TABLE
+61	67	ICP-MS	experimental_method	Fractions from SEC were collected, acidified and analysed by ICP-MS.	TABLE
+0	8	EncFtnsH	protein	EncFtnsH concentration was calculated based on the presence of two SeMet per mature monomer.	TABLE
+51	62	presence of	protein_state	EncFtnsH concentration was calculated based on the presence of two SeMet per mature monomer.	TABLE
+67	72	SeMet	chemical	EncFtnsH concentration was calculated based on the presence of two SeMet per mature monomer.	TABLE
+77	83	mature	protein_state	EncFtnsH concentration was calculated based on the presence of two SeMet per mature monomer.	TABLE
+84	91	monomer	oligomeric_state	EncFtnsH concentration was calculated based on the presence of two SeMet per mature monomer.	TABLE
+31	39	EncFtnsH	protein	These data were collected from EncFtnsH fractions from a single gel-filtration run.	TABLE
+64	78	gel-filtration	experimental_method	These data were collected from EncFtnsH fractions from a single gel-filtration run.	TABLE
+5	13	EncFtnsH	protein	"Peak	EncFtnsHretention volume (ml)	Element concentration (µM)	Derived EncFtnsHconcentration (µM)	Derived Fe/ EncFtnsH monomer	 	Ca	Fe	Zn	Se	 	Decamer	66.5	n.d."	TABLE
+70	78	EncFtnsH	protein	"Peak	EncFtnsHretention volume (ml)	Element concentration (µM)	Derived EncFtnsHconcentration (µM)	Derived Fe/ EncFtnsH monomer	 	Ca	Fe	Zn	Se	 	Decamer	66.5	n.d."	TABLE
+105	107	Fe	chemical	"Peak	EncFtnsHretention volume (ml)	Element concentration (µM)	Derived EncFtnsHconcentration (µM)	Derived Fe/ EncFtnsH monomer	 	Ca	Fe	Zn	Se	 	Decamer	66.5	n.d."	TABLE
+109	117	EncFtnsH	protein	"Peak	EncFtnsHretention volume (ml)	Element concentration (µM)	Derived EncFtnsHconcentration (µM)	Derived Fe/ EncFtnsH monomer	 	Ca	Fe	Zn	Se	 	Decamer	66.5	n.d."	TABLE
+118	125	monomer	oligomeric_state	"Peak	EncFtnsHretention volume (ml)	Element concentration (µM)	Derived EncFtnsHconcentration (µM)	Derived Fe/ EncFtnsH monomer	 	Ca	Fe	Zn	Se	 	Decamer	66.5	n.d."	TABLE
+128	130	Ca	chemical	"Peak	EncFtnsHretention volume (ml)	Element concentration (µM)	Derived EncFtnsHconcentration (µM)	Derived Fe/ EncFtnsH monomer	 	Ca	Fe	Zn	Se	 	Decamer	66.5	n.d."	TABLE
+131	133	Fe	chemical	"Peak	EncFtnsHretention volume (ml)	Element concentration (µM)	Derived EncFtnsHconcentration (µM)	Derived Fe/ EncFtnsH monomer	 	Ca	Fe	Zn	Se	 	Decamer	66.5	n.d."	TABLE
+134	136	Zn	chemical	"Peak	EncFtnsHretention volume (ml)	Element concentration (µM)	Derived EncFtnsHconcentration (µM)	Derived Fe/ EncFtnsH monomer	 	Ca	Fe	Zn	Se	 	Decamer	66.5	n.d."	TABLE
+137	139	Se	chemical	"Peak	EncFtnsHretention volume (ml)	Element concentration (µM)	Derived EncFtnsHconcentration (µM)	Derived Fe/ EncFtnsH monomer	 	Ca	Fe	Zn	Se	 	Decamer	66.5	n.d."	TABLE
+142	149	Decamer	oligomeric_state	"Peak	EncFtnsHretention volume (ml)	Element concentration (µM)	Derived EncFtnsHconcentration (µM)	Derived Fe/ EncFtnsH monomer	 	Ca	Fe	Zn	Se	 	Decamer	66.5	n.d."	TABLE
+13	21	EncFtnsH	protein	Estimates of EncFtnsH molecular weight from SEC-MALLS analysis.	TABLE
+22	38	molecular weight	evidence	Estimates of EncFtnsH molecular weight from SEC-MALLS analysis.	TABLE
+44	53	SEC-MALLS	experimental_method	Estimates of EncFtnsH molecular weight from SEC-MALLS analysis.	TABLE
+0	8	EncFtnsH	protein	EncFtnsH was purified from E. coli BL21(DE3) grown in minimal medium (MM) by nickel affinity chromatography and size-exclusion chromatography.	TABLE
+27	44	E. coli BL21(DE3)	species	EncFtnsH was purified from E. coli BL21(DE3) grown in minimal medium (MM) by nickel affinity chromatography and size-exclusion chromatography.	TABLE
+54	68	minimal medium	experimental_method	EncFtnsH was purified from E. coli BL21(DE3) grown in minimal medium (MM) by nickel affinity chromatography and size-exclusion chromatography.	TABLE
+70	72	MM	experimental_method	EncFtnsH was purified from E. coli BL21(DE3) grown in minimal medium (MM) by nickel affinity chromatography and size-exclusion chromatography.	TABLE
+77	107	nickel affinity chromatography	experimental_method	EncFtnsH was purified from E. coli BL21(DE3) grown in minimal medium (MM) by nickel affinity chromatography and size-exclusion chromatography.	TABLE
+112	141	size-exclusion chromatography	experimental_method	EncFtnsH was purified from E. coli BL21(DE3) grown in minimal medium (MM) by nickel affinity chromatography and size-exclusion chromatography.	TABLE
+19	24	peaks	evidence	Fractions from two peaks (decamer and monomer) were pooled separately (Figure 1C) and analysed by SEC-MALLS using a Superdex 200 10/300 GL column (GE Healthcare) and Viscotek SEC-MALLS instruments (Malvern Instruments) (Figure 2C).	TABLE
+26	33	decamer	oligomeric_state	Fractions from two peaks (decamer and monomer) were pooled separately (Figure 1C) and analysed by SEC-MALLS using a Superdex 200 10/300 GL column (GE Healthcare) and Viscotek SEC-MALLS instruments (Malvern Instruments) (Figure 2C).	TABLE
+38	45	monomer	oligomeric_state	Fractions from two peaks (decamer and monomer) were pooled separately (Figure 1C) and analysed by SEC-MALLS using a Superdex 200 10/300 GL column (GE Healthcare) and Viscotek SEC-MALLS instruments (Malvern Instruments) (Figure 2C).	TABLE
+98	107	SEC-MALLS	experimental_method	Fractions from two peaks (decamer and monomer) were pooled separately (Figure 1C) and analysed by SEC-MALLS using a Superdex 200 10/300 GL column (GE Healthcare) and Viscotek SEC-MALLS instruments (Malvern Instruments) (Figure 2C).	TABLE
+175	184	SEC-MALLS	experimental_method	Fractions from two peaks (decamer and monomer) were pooled separately (Figure 1C) and analysed by SEC-MALLS using a Superdex 200 10/300 GL column (GE Healthcare) and Viscotek SEC-MALLS instruments (Malvern Instruments) (Figure 2C).	TABLE
+4	11	decamer	oligomeric_state	The decamer and monomer peaks were both symmetric and monodisperse, allowing the estimation of the molecular weight of the species in these fractions.	TABLE
+16	23	monomer	oligomeric_state	The decamer and monomer peaks were both symmetric and monodisperse, allowing the estimation of the molecular weight of the species in these fractions.	TABLE
+24	29	peaks	evidence	The decamer and monomer peaks were both symmetric and monodisperse, allowing the estimation of the molecular weight of the species in these fractions.	TABLE
+99	115	molecular weight	evidence	The decamer and monomer peaks were both symmetric and monodisperse, allowing the estimation of the molecular weight of the species in these fractions.	TABLE
+25	34	SEC-MALLS	experimental_method	The proteins analyzed by SEC-MALLS came from single protein preparation.	TABLE
+0	16	Molecular Weight	evidence	"Molecular Weight (kDa)	Decamer peak	Monomer peak	 	Theoretical	133	13	 	EncFtnsH-decamer fractions	132	15	 	EncFtnsH-monomer fractions	126	13	 	"	TABLE
+23	30	Decamer	oligomeric_state	"Molecular Weight (kDa)	Decamer peak	Monomer peak	 	Theoretical	133	13	 	EncFtnsH-decamer fractions	132	15	 	EncFtnsH-monomer fractions	126	13	 	"	TABLE
+36	43	Monomer	oligomeric_state	"Molecular Weight (kDa)	Decamer peak	Monomer peak	 	Theoretical	133	13	 	EncFtnsH-decamer fractions	132	15	 	EncFtnsH-monomer fractions	126	13	 	"	TABLE
+72	80	EncFtnsH	protein	"Molecular Weight (kDa)	Decamer peak	Monomer peak	 	Theoretical	133	13	 	EncFtnsH-decamer fractions	132	15	 	EncFtnsH-monomer fractions	126	13	 	"	TABLE
+81	88	decamer	oligomeric_state	"Molecular Weight (kDa)	Decamer peak	Monomer peak	 	Theoretical	133	13	 	EncFtnsH-decamer fractions	132	15	 	EncFtnsH-monomer fractions	126	13	 	"	TABLE
+108	116	EncFtnsH	protein	"Molecular Weight (kDa)	Decamer peak	Monomer peak	 	Theoretical	133	13	 	EncFtnsH-decamer fractions	132	15	 	EncFtnsH-monomer fractions	126	13	 	"	TABLE
+117	124	monomer	oligomeric_state	"Molecular Weight (kDa)	Decamer peak	Monomer peak	 	Theoretical	133	13	 	EncFtnsH-decamer fractions	132	15	 	EncFtnsH-monomer fractions	126	13	 	"	TABLE
+24	33	R. rubrum	species	We purified recombinant R. rubrum EncFtn as both the full-length sequence (140 amino acids) and a truncated C-terminal hexahistidine-tagged variant (amino acids 1–96 plus the tag; herein EncFtnsH).	RESULTS
+34	40	EncFtn	protein	We purified recombinant R. rubrum EncFtn as both the full-length sequence (140 amino acids) and a truncated C-terminal hexahistidine-tagged variant (amino acids 1–96 plus the tag; herein EncFtnsH).	RESULTS
+53	64	full-length	protein_state	We purified recombinant R. rubrum EncFtn as both the full-length sequence (140 amino acids) and a truncated C-terminal hexahistidine-tagged variant (amino acids 1–96 plus the tag; herein EncFtnsH).	RESULTS
+75	90	140 amino acids	residue_range	We purified recombinant R. rubrum EncFtn as both the full-length sequence (140 amino acids) and a truncated C-terminal hexahistidine-tagged variant (amino acids 1–96 plus the tag; herein EncFtnsH).	RESULTS
+98	107	truncated	protein_state	We purified recombinant R. rubrum EncFtn as both the full-length sequence (140 amino acids) and a truncated C-terminal hexahistidine-tagged variant (amino acids 1–96 plus the tag; herein EncFtnsH).	RESULTS
+119	139	hexahistidine-tagged	protein_state	We purified recombinant R. rubrum EncFtn as both the full-length sequence (140 amino acids) and a truncated C-terminal hexahistidine-tagged variant (amino acids 1–96 plus the tag; herein EncFtnsH).	RESULTS
+161	165	1–96	residue_range	We purified recombinant R. rubrum EncFtn as both the full-length sequence (140 amino acids) and a truncated C-terminal hexahistidine-tagged variant (amino acids 1–96 plus the tag; herein EncFtnsH).	RESULTS
+187	195	EncFtnsH	protein	We purified recombinant R. rubrum EncFtn as both the full-length sequence (140 amino acids) and a truncated C-terminal hexahistidine-tagged variant (amino acids 1–96 plus the tag; herein EncFtnsH).	RESULTS
+18	33	elution profile	evidence	In both cases the elution profile from size-exclusion chromatography (SEC) displayed two peaks (Figure 2A).	RESULTS
+39	68	size-exclusion chromatography	experimental_method	In both cases the elution profile from size-exclusion chromatography (SEC) displayed two peaks (Figure 2A).	RESULTS
+70	73	SEC	experimental_method	In both cases the elution profile from size-exclusion chromatography (SEC) displayed two peaks (Figure 2A).	RESULTS
+89	94	peaks	evidence	In both cases the elution profile from size-exclusion chromatography (SEC) displayed two peaks (Figure 2A).	RESULTS
+0	8	SDS-PAGE	experimental_method	SDS-PAGE analysis of fractions from these peaks showed that the high molecular weight peak was partially resistant to SDS and heat-induced denaturation; in contrast, the low molecular weight peak was consistent with monomeric mass of 13 kDa (Figure 2B).	RESULTS
+42	47	peaks	evidence	SDS-PAGE analysis of fractions from these peaks showed that the high molecular weight peak was partially resistant to SDS and heat-induced denaturation; in contrast, the low molecular weight peak was consistent with monomeric mass of 13 kDa (Figure 2B).	RESULTS
+69	85	molecular weight	evidence	SDS-PAGE analysis of fractions from these peaks showed that the high molecular weight peak was partially resistant to SDS and heat-induced denaturation; in contrast, the low molecular weight peak was consistent with monomeric mass of 13 kDa (Figure 2B).	RESULTS
+174	190	molecular weight	evidence	SDS-PAGE analysis of fractions from these peaks showed that the high molecular weight peak was partially resistant to SDS and heat-induced denaturation; in contrast, the low molecular weight peak was consistent with monomeric mass of 13 kDa (Figure 2B).	RESULTS
+216	225	monomeric	oligomeric_state	SDS-PAGE analysis of fractions from these peaks showed that the high molecular weight peak was partially resistant to SDS and heat-induced denaturation; in contrast, the low molecular weight peak was consistent with monomeric mass of 13 kDa (Figure 2B).	RESULTS
+0	33	MALDI peptide mass fingerprinting	experimental_method	MALDI peptide mass fingerprinting of these bands confirmed the identity of both as EncFtn.	RESULTS
+83	89	EncFtn	protein	MALDI peptide mass fingerprinting of these bands confirmed the identity of both as EncFtn.	RESULTS
+0	44	Inductively coupled plasma mass spectrometry	experimental_method	Inductively coupled plasma mass spectrometry (ICP-MS) analysis of the SEC fractions showed 100 times more iron in the oligomeric fraction than the monomer (Figure 2A, blue scatter points; Table 1), suggesting that EncFtn oligomerization is associated with iron binding.	RESULTS
+46	52	ICP-MS	experimental_method	Inductively coupled plasma mass spectrometry (ICP-MS) analysis of the SEC fractions showed 100 times more iron in the oligomeric fraction than the monomer (Figure 2A, blue scatter points; Table 1), suggesting that EncFtn oligomerization is associated with iron binding.	RESULTS
+70	73	SEC	experimental_method	Inductively coupled plasma mass spectrometry (ICP-MS) analysis of the SEC fractions showed 100 times more iron in the oligomeric fraction than the monomer (Figure 2A, blue scatter points; Table 1), suggesting that EncFtn oligomerization is associated with iron binding.	RESULTS
+106	110	iron	chemical	Inductively coupled plasma mass spectrometry (ICP-MS) analysis of the SEC fractions showed 100 times more iron in the oligomeric fraction than the monomer (Figure 2A, blue scatter points; Table 1), suggesting that EncFtn oligomerization is associated with iron binding.	RESULTS
+147	154	monomer	oligomeric_state	Inductively coupled plasma mass spectrometry (ICP-MS) analysis of the SEC fractions showed 100 times more iron in the oligomeric fraction than the monomer (Figure 2A, blue scatter points; Table 1), suggesting that EncFtn oligomerization is associated with iron binding.	RESULTS
+214	220	EncFtn	protein	Inductively coupled plasma mass spectrometry (ICP-MS) analysis of the SEC fractions showed 100 times more iron in the oligomeric fraction than the monomer (Figure 2A, blue scatter points; Table 1), suggesting that EncFtn oligomerization is associated with iron binding.	RESULTS
+256	260	iron	chemical	Inductively coupled plasma mass spectrometry (ICP-MS) analysis of the SEC fractions showed 100 times more iron in the oligomeric fraction than the monomer (Figure 2A, blue scatter points; Table 1), suggesting that EncFtn oligomerization is associated with iron binding.	RESULTS
+26	30	iron	chemical	In order to determine the iron-loading stoichiometry in the EncFtn complex, further ICP-MS experiments were performed using selenomethionine (SeMet)-labelled protein EncFtn (Table 1).	RESULTS
+60	66	EncFtn	protein	In order to determine the iron-loading stoichiometry in the EncFtn complex, further ICP-MS experiments were performed using selenomethionine (SeMet)-labelled protein EncFtn (Table 1).	RESULTS
+84	90	ICP-MS	experimental_method	In order to determine the iron-loading stoichiometry in the EncFtn complex, further ICP-MS experiments were performed using selenomethionine (SeMet)-labelled protein EncFtn (Table 1).	RESULTS
+124	140	selenomethionine	chemical	In order to determine the iron-loading stoichiometry in the EncFtn complex, further ICP-MS experiments were performed using selenomethionine (SeMet)-labelled protein EncFtn (Table 1).	RESULTS
+142	147	SeMet	chemical	In order to determine the iron-loading stoichiometry in the EncFtn complex, further ICP-MS experiments were performed using selenomethionine (SeMet)-labelled protein EncFtn (Table 1).	RESULTS
+166	172	EncFtn	protein	In order to determine the iron-loading stoichiometry in the EncFtn complex, further ICP-MS experiments were performed using selenomethionine (SeMet)-labelled protein EncFtn (Table 1).	RESULTS
+96	105	classical	protein_state	In these experiments, we observed sub-stoichiometric metal binding, which is in contrast to the classical ferritins.	RESULTS
+106	115	ferritins	protein_type	In these experiments, we observed sub-stoichiometric metal binding, which is in contrast to the classical ferritins.	RESULTS
+0	29	Size-exclusion chromatography	experimental_method	Size-exclusion chromatography with multi-angle laser light scattering (SEC-MALLS) analysis of samples taken from each peak gave calculated molecular weights consistent with a decamer for the high molecular weight peak and a monomer for the low molecular weight peak (Figure 2C, Table 2).	RESULTS
+35	69	multi-angle laser light scattering	experimental_method	Size-exclusion chromatography with multi-angle laser light scattering (SEC-MALLS) analysis of samples taken from each peak gave calculated molecular weights consistent with a decamer for the high molecular weight peak and a monomer for the low molecular weight peak (Figure 2C, Table 2).	RESULTS
+71	80	SEC-MALLS	experimental_method	Size-exclusion chromatography with multi-angle laser light scattering (SEC-MALLS) analysis of samples taken from each peak gave calculated molecular weights consistent with a decamer for the high molecular weight peak and a monomer for the low molecular weight peak (Figure 2C, Table 2).	RESULTS
+175	182	decamer	oligomeric_state	Size-exclusion chromatography with multi-angle laser light scattering (SEC-MALLS) analysis of samples taken from each peak gave calculated molecular weights consistent with a decamer for the high molecular weight peak and a monomer for the low molecular weight peak (Figure 2C, Table 2).	RESULTS
+196	212	molecular weight	evidence	Size-exclusion chromatography with multi-angle laser light scattering (SEC-MALLS) analysis of samples taken from each peak gave calculated molecular weights consistent with a decamer for the high molecular weight peak and a monomer for the low molecular weight peak (Figure 2C, Table 2).	RESULTS
+224	231	monomer	oligomeric_state	Size-exclusion chromatography with multi-angle laser light scattering (SEC-MALLS) analysis of samples taken from each peak gave calculated molecular weights consistent with a decamer for the high molecular weight peak and a monomer for the low molecular weight peak (Figure 2C, Table 2).	RESULTS
+244	260	molecular weight	evidence	Size-exclusion chromatography with multi-angle laser light scattering (SEC-MALLS) analysis of samples taken from each peak gave calculated molecular weights consistent with a decamer for the high molecular weight peak and a monomer for the low molecular weight peak (Figure 2C, Table 2).	RESULTS
+48	56	EncFtnsH	protein	Effect of metal ions on the oligomeric state of EncFtnsH in solution.	FIG
+6	14	EncFtnsH	protein	(A/B) EncFtnsH-monomer was incubated with one mole equivalent of various metal salts for two hours prior to analytical gel-filtration using a Superdex 200 PC 3.2/30 column.	FIG
+15	22	monomer	oligomeric_state	(A/B) EncFtnsH-monomer was incubated with one mole equivalent of various metal salts for two hours prior to analytical gel-filtration using a Superdex 200 PC 3.2/30 column.	FIG
+27	36	incubated	experimental_method	(A/B) EncFtnsH-monomer was incubated with one mole equivalent of various metal salts for two hours prior to analytical gel-filtration using a Superdex 200 PC 3.2/30 column.	FIG
+108	133	analytical gel-filtration	experimental_method	(A/B) EncFtnsH-monomer was incubated with one mole equivalent of various metal salts for two hours prior to analytical gel-filtration using a Superdex 200 PC 3.2/30 column.	FIG
+0	4	Co2+	chemical	Co2+ and Zn2+ induced the formation of the decameric form of EncFtnsH; while Mn2+, Mg2+ and Fe3+ did not significantly alter the oligomeric state of EncFtnsH.	FIG
+9	13	Zn2+	chemical	Co2+ and Zn2+ induced the formation of the decameric form of EncFtnsH; while Mn2+, Mg2+ and Fe3+ did not significantly alter the oligomeric state of EncFtnsH.	FIG
+43	52	decameric	oligomeric_state	Co2+ and Zn2+ induced the formation of the decameric form of EncFtnsH; while Mn2+, Mg2+ and Fe3+ did not significantly alter the oligomeric state of EncFtnsH.	FIG
+61	69	EncFtnsH	protein	Co2+ and Zn2+ induced the formation of the decameric form of EncFtnsH; while Mn2+, Mg2+ and Fe3+ did not significantly alter the oligomeric state of EncFtnsH.	FIG
+77	81	Mn2+	chemical	Co2+ and Zn2+ induced the formation of the decameric form of EncFtnsH; while Mn2+, Mg2+ and Fe3+ did not significantly alter the oligomeric state of EncFtnsH.	FIG
+83	87	Mg2+	chemical	Co2+ and Zn2+ induced the formation of the decameric form of EncFtnsH; while Mn2+, Mg2+ and Fe3+ did not significantly alter the oligomeric state of EncFtnsH.	FIG
+92	96	Fe3+	chemical	Co2+ and Zn2+ induced the formation of the decameric form of EncFtnsH; while Mn2+, Mg2+ and Fe3+ did not significantly alter the oligomeric state of EncFtnsH.	FIG
+149	157	EncFtnsH	protein	Co2+ and Zn2+ induced the formation of the decameric form of EncFtnsH; while Mn2+, Mg2+ and Fe3+ did not significantly alter the oligomeric state of EncFtnsH.	FIG
+0	4	PAGE	experimental_method	PAGE analysis of the effect of metal ions on the oligomeric state of EncFtnsH.	FIG
+69	77	EncFtnsH	protein	PAGE analysis of the effect of metal ions on the oligomeric state of EncFtnsH.	FIG
+6	14	EncFtnsH	protein	50 µM EncFtnsH monomer or decamer samples were mixed with equal molar metal ions including Fe2+, Co2+, Zn2+, Mn2+, Ca2+, Mg2+ and Fe3+, which were analyzed by Native PAGE alongside SDS-PAGE.	FIG
+15	22	monomer	oligomeric_state	50 µM EncFtnsH monomer or decamer samples were mixed with equal molar metal ions including Fe2+, Co2+, Zn2+, Mn2+, Ca2+, Mg2+ and Fe3+, which were analyzed by Native PAGE alongside SDS-PAGE.	FIG
+26	33	decamer	oligomeric_state	50 µM EncFtnsH monomer or decamer samples were mixed with equal molar metal ions including Fe2+, Co2+, Zn2+, Mn2+, Ca2+, Mg2+ and Fe3+, which were analyzed by Native PAGE alongside SDS-PAGE.	FIG
+91	96	Fe2+,	chemical	50 µM EncFtnsH monomer or decamer samples were mixed with equal molar metal ions including Fe2+, Co2+, Zn2+, Mn2+, Ca2+, Mg2+ and Fe3+, which were analyzed by Native PAGE alongside SDS-PAGE.	FIG
+97	102	Co2+,	chemical	50 µM EncFtnsH monomer or decamer samples were mixed with equal molar metal ions including Fe2+, Co2+, Zn2+, Mn2+, Ca2+, Mg2+ and Fe3+, which were analyzed by Native PAGE alongside SDS-PAGE.	FIG
+103	108	Zn2+,	chemical	50 µM EncFtnsH monomer or decamer samples were mixed with equal molar metal ions including Fe2+, Co2+, Zn2+, Mn2+, Ca2+, Mg2+ and Fe3+, which were analyzed by Native PAGE alongside SDS-PAGE.	FIG
+109	114	Mn2+,	chemical	50 µM EncFtnsH monomer or decamer samples were mixed with equal molar metal ions including Fe2+, Co2+, Zn2+, Mn2+, Ca2+, Mg2+ and Fe3+, which were analyzed by Native PAGE alongside SDS-PAGE.	FIG
+115	120	Ca2+,	chemical	50 µM EncFtnsH monomer or decamer samples were mixed with equal molar metal ions including Fe2+, Co2+, Zn2+, Mn2+, Ca2+, Mg2+ and Fe3+, which were analyzed by Native PAGE alongside SDS-PAGE.	FIG
+121	125	Mg2+	chemical	50 µM EncFtnsH monomer or decamer samples were mixed with equal molar metal ions including Fe2+, Co2+, Zn2+, Mn2+, Ca2+, Mg2+ and Fe3+, which were analyzed by Native PAGE alongside SDS-PAGE.	FIG
+130	135	Fe3+,	chemical	50 µM EncFtnsH monomer or decamer samples were mixed with equal molar metal ions including Fe2+, Co2+, Zn2+, Mn2+, Ca2+, Mg2+ and Fe3+, which were analyzed by Native PAGE alongside SDS-PAGE.	FIG
+159	170	Native PAGE	experimental_method	50 µM EncFtnsH monomer or decamer samples were mixed with equal molar metal ions including Fe2+, Co2+, Zn2+, Mn2+, Ca2+, Mg2+ and Fe3+, which were analyzed by Native PAGE alongside SDS-PAGE.	FIG
+181	189	SDS-PAGE	experimental_method	50 µM EncFtnsH monomer or decamer samples were mixed with equal molar metal ions including Fe2+, Co2+, Zn2+, Mn2+, Ca2+, Mg2+ and Fe3+, which were analyzed by Native PAGE alongside SDS-PAGE.	FIG
+9	20	Native PAGE	experimental_method	 (A) 10% Native PAGE analysis of EncFtnsH monomer fractions mixed with various metal solutions; (B) 10% Native PAGE analysis of EncFtnsH decamer fractions mixed with various metal solutions; (C) 15% SDS-PAGE analysis on the mixtures of EncFtnsH monomer fractions and metal solutions; (D) 15% SDS-PAGE analysis on the mixtures of EncFtnsH decamer fractions and metal solutions.	FIG
+33	41	EncFtnsH	protein	 (A) 10% Native PAGE analysis of EncFtnsH monomer fractions mixed with various metal solutions; (B) 10% Native PAGE analysis of EncFtnsH decamer fractions mixed with various metal solutions; (C) 15% SDS-PAGE analysis on the mixtures of EncFtnsH monomer fractions and metal solutions; (D) 15% SDS-PAGE analysis on the mixtures of EncFtnsH decamer fractions and metal solutions.	FIG
+42	49	monomer	oligomeric_state	 (A) 10% Native PAGE analysis of EncFtnsH monomer fractions mixed with various metal solutions; (B) 10% Native PAGE analysis of EncFtnsH decamer fractions mixed with various metal solutions; (C) 15% SDS-PAGE analysis on the mixtures of EncFtnsH monomer fractions and metal solutions; (D) 15% SDS-PAGE analysis on the mixtures of EncFtnsH decamer fractions and metal solutions.	FIG
+104	115	Native PAGE	experimental_method	 (A) 10% Native PAGE analysis of EncFtnsH monomer fractions mixed with various metal solutions; (B) 10% Native PAGE analysis of EncFtnsH decamer fractions mixed with various metal solutions; (C) 15% SDS-PAGE analysis on the mixtures of EncFtnsH monomer fractions and metal solutions; (D) 15% SDS-PAGE analysis on the mixtures of EncFtnsH decamer fractions and metal solutions.	FIG
+128	136	EncFtnsH	protein	 (A) 10% Native PAGE analysis of EncFtnsH monomer fractions mixed with various metal solutions; (B) 10% Native PAGE analysis of EncFtnsH decamer fractions mixed with various metal solutions; (C) 15% SDS-PAGE analysis on the mixtures of EncFtnsH monomer fractions and metal solutions; (D) 15% SDS-PAGE analysis on the mixtures of EncFtnsH decamer fractions and metal solutions.	FIG
+137	144	decamer	oligomeric_state	 (A) 10% Native PAGE analysis of EncFtnsH monomer fractions mixed with various metal solutions; (B) 10% Native PAGE analysis of EncFtnsH decamer fractions mixed with various metal solutions; (C) 15% SDS-PAGE analysis on the mixtures of EncFtnsH monomer fractions and metal solutions; (D) 15% SDS-PAGE analysis on the mixtures of EncFtnsH decamer fractions and metal solutions.	FIG
+199	207	SDS-PAGE	experimental_method	 (A) 10% Native PAGE analysis of EncFtnsH monomer fractions mixed with various metal solutions; (B) 10% Native PAGE analysis of EncFtnsH decamer fractions mixed with various metal solutions; (C) 15% SDS-PAGE analysis on the mixtures of EncFtnsH monomer fractions and metal solutions; (D) 15% SDS-PAGE analysis on the mixtures of EncFtnsH decamer fractions and metal solutions.	FIG
+236	244	EncFtnsH	protein	 (A) 10% Native PAGE analysis of EncFtnsH monomer fractions mixed with various metal solutions; (B) 10% Native PAGE analysis of EncFtnsH decamer fractions mixed with various metal solutions; (C) 15% SDS-PAGE analysis on the mixtures of EncFtnsH monomer fractions and metal solutions; (D) 15% SDS-PAGE analysis on the mixtures of EncFtnsH decamer fractions and metal solutions.	FIG
+245	252	monomer	oligomeric_state	 (A) 10% Native PAGE analysis of EncFtnsH monomer fractions mixed with various metal solutions; (B) 10% Native PAGE analysis of EncFtnsH decamer fractions mixed with various metal solutions; (C) 15% SDS-PAGE analysis on the mixtures of EncFtnsH monomer fractions and metal solutions; (D) 15% SDS-PAGE analysis on the mixtures of EncFtnsH decamer fractions and metal solutions.	FIG
+292	300	SDS-PAGE	experimental_method	 (A) 10% Native PAGE analysis of EncFtnsH monomer fractions mixed with various metal solutions; (B) 10% Native PAGE analysis of EncFtnsH decamer fractions mixed with various metal solutions; (C) 15% SDS-PAGE analysis on the mixtures of EncFtnsH monomer fractions and metal solutions; (D) 15% SDS-PAGE analysis on the mixtures of EncFtnsH decamer fractions and metal solutions.	FIG
+329	337	EncFtnsH	protein	 (A) 10% Native PAGE analysis of EncFtnsH monomer fractions mixed with various metal solutions; (B) 10% Native PAGE analysis of EncFtnsH decamer fractions mixed with various metal solutions; (C) 15% SDS-PAGE analysis on the mixtures of EncFtnsH monomer fractions and metal solutions; (D) 15% SDS-PAGE analysis on the mixtures of EncFtnsH decamer fractions and metal solutions.	FIG
+338	345	decamer	oligomeric_state	 (A) 10% Native PAGE analysis of EncFtnsH monomer fractions mixed with various metal solutions; (B) 10% Native PAGE analysis of EncFtnsH decamer fractions mixed with various metal solutions; (C) 15% SDS-PAGE analysis on the mixtures of EncFtnsH monomer fractions and metal solutions; (D) 15% SDS-PAGE analysis on the mixtures of EncFtnsH decamer fractions and metal solutions.	FIG
+10	14	Fe2+	chemical	Effect of Fe2+ and protein concentration on the oligomeric state of EncFtnsH in solution.	FIG
+68	76	EncFtnsH	protein	Effect of Fe2+ and protein concentration on the oligomeric state of EncFtnsH in solution.	FIG
+16	24	EncFtnsH	protein	(A) Recombinant EncFtnsH was purified by Gel filtration Superdex 200 chromatography from E. coli BL21(DE3) grown in MM or in MM supplemented with 1 mM Fe(NH4)2(SO4)2 (MM+Fe2+).	FIG
+41	55	Gel filtration	experimental_method	(A) Recombinant EncFtnsH was purified by Gel filtration Superdex 200 chromatography from E. coli BL21(DE3) grown in MM or in MM supplemented with 1 mM Fe(NH4)2(SO4)2 (MM+Fe2+).	FIG
+89	106	E. coli BL21(DE3)	species	(A) Recombinant EncFtnsH was purified by Gel filtration Superdex 200 chromatography from E. coli BL21(DE3) grown in MM or in MM supplemented with 1 mM Fe(NH4)2(SO4)2 (MM+Fe2+).	FIG
+116	118	MM	experimental_method	(A) Recombinant EncFtnsH was purified by Gel filtration Superdex 200 chromatography from E. coli BL21(DE3) grown in MM or in MM supplemented with 1 mM Fe(NH4)2(SO4)2 (MM+Fe2+).	FIG
+125	127	MM	experimental_method	(A) Recombinant EncFtnsH was purified by Gel filtration Superdex 200 chromatography from E. coli BL21(DE3) grown in MM or in MM supplemented with 1 mM Fe(NH4)2(SO4)2 (MM+Fe2+).	FIG
+151	165	Fe(NH4)2(SO4)2	chemical	(A) Recombinant EncFtnsH was purified by Gel filtration Superdex 200 chromatography from E. coli BL21(DE3) grown in MM or in MM supplemented with 1 mM Fe(NH4)2(SO4)2 (MM+Fe2+).	FIG
+167	169	MM	experimental_method	(A) Recombinant EncFtnsH was purified by Gel filtration Superdex 200 chromatography from E. coli BL21(DE3) grown in MM or in MM supplemented with 1 mM Fe(NH4)2(SO4)2 (MM+Fe2+).	FIG
+170	174	Fe2+	chemical	(A) Recombinant EncFtnsH was purified by Gel filtration Superdex 200 chromatography from E. coli BL21(DE3) grown in MM or in MM supplemented with 1 mM Fe(NH4)2(SO4)2 (MM+Fe2+).	FIG
+23	30	decamer	oligomeric_state	A higher proportion of decamer (peak between 65 and 75 ml) is seen in the sample purified from MM+Fe2+ compared to EncFtnsH-MM, indicating that Fe2+ facilitates the multimerization of EncFtnsH in vivo. (B) EncFtnsH-monomer was incubated with one molar equivalent of Fe2+ salts for two hours prior to analytical gel-filtration using a Superdex 200 PC 3.2/30 column (GE Healthcare).	FIG
+95	97	MM	experimental_method	A higher proportion of decamer (peak between 65 and 75 ml) is seen in the sample purified from MM+Fe2+ compared to EncFtnsH-MM, indicating that Fe2+ facilitates the multimerization of EncFtnsH in vivo. (B) EncFtnsH-monomer was incubated with one molar equivalent of Fe2+ salts for two hours prior to analytical gel-filtration using a Superdex 200 PC 3.2/30 column (GE Healthcare).	FIG
+98	102	Fe2+	chemical	A higher proportion of decamer (peak between 65 and 75 ml) is seen in the sample purified from MM+Fe2+ compared to EncFtnsH-MM, indicating that Fe2+ facilitates the multimerization of EncFtnsH in vivo. (B) EncFtnsH-monomer was incubated with one molar equivalent of Fe2+ salts for two hours prior to analytical gel-filtration using a Superdex 200 PC 3.2/30 column (GE Healthcare).	FIG
+115	123	EncFtnsH	protein	A higher proportion of decamer (peak between 65 and 75 ml) is seen in the sample purified from MM+Fe2+ compared to EncFtnsH-MM, indicating that Fe2+ facilitates the multimerization of EncFtnsH in vivo. (B) EncFtnsH-monomer was incubated with one molar equivalent of Fe2+ salts for two hours prior to analytical gel-filtration using a Superdex 200 PC 3.2/30 column (GE Healthcare).	FIG
+124	126	MM	experimental_method	A higher proportion of decamer (peak between 65 and 75 ml) is seen in the sample purified from MM+Fe2+ compared to EncFtnsH-MM, indicating that Fe2+ facilitates the multimerization of EncFtnsH in vivo. (B) EncFtnsH-monomer was incubated with one molar equivalent of Fe2+ salts for two hours prior to analytical gel-filtration using a Superdex 200 PC 3.2/30 column (GE Healthcare).	FIG
+144	148	Fe2+	chemical	A higher proportion of decamer (peak between 65 and 75 ml) is seen in the sample purified from MM+Fe2+ compared to EncFtnsH-MM, indicating that Fe2+ facilitates the multimerization of EncFtnsH in vivo. (B) EncFtnsH-monomer was incubated with one molar equivalent of Fe2+ salts for two hours prior to analytical gel-filtration using a Superdex 200 PC 3.2/30 column (GE Healthcare).	FIG
+184	192	EncFtnsH	protein	A higher proportion of decamer (peak between 65 and 75 ml) is seen in the sample purified from MM+Fe2+ compared to EncFtnsH-MM, indicating that Fe2+ facilitates the multimerization of EncFtnsH in vivo. (B) EncFtnsH-monomer was incubated with one molar equivalent of Fe2+ salts for two hours prior to analytical gel-filtration using a Superdex 200 PC 3.2/30 column (GE Healthcare).	FIG
+206	214	EncFtnsH	protein	A higher proportion of decamer (peak between 65 and 75 ml) is seen in the sample purified from MM+Fe2+ compared to EncFtnsH-MM, indicating that Fe2+ facilitates the multimerization of EncFtnsH in vivo. (B) EncFtnsH-monomer was incubated with one molar equivalent of Fe2+ salts for two hours prior to analytical gel-filtration using a Superdex 200 PC 3.2/30 column (GE Healthcare).	FIG
+215	222	monomer	oligomeric_state	A higher proportion of decamer (peak between 65 and 75 ml) is seen in the sample purified from MM+Fe2+ compared to EncFtnsH-MM, indicating that Fe2+ facilitates the multimerization of EncFtnsH in vivo. (B) EncFtnsH-monomer was incubated with one molar equivalent of Fe2+ salts for two hours prior to analytical gel-filtration using a Superdex 200 PC 3.2/30 column (GE Healthcare).	FIG
+266	270	Fe2+	chemical	A higher proportion of decamer (peak between 65 and 75 ml) is seen in the sample purified from MM+Fe2+ compared to EncFtnsH-MM, indicating that Fe2+ facilitates the multimerization of EncFtnsH in vivo. (B) EncFtnsH-monomer was incubated with one molar equivalent of Fe2+ salts for two hours prior to analytical gel-filtration using a Superdex 200 PC 3.2/30 column (GE Healthcare).	FIG
+300	325	analytical gel-filtration	experimental_method	A higher proportion of decamer (peak between 65 and 75 ml) is seen in the sample purified from MM+Fe2+ compared to EncFtnsH-MM, indicating that Fe2+ facilitates the multimerization of EncFtnsH in vivo. (B) EncFtnsH-monomer was incubated with one molar equivalent of Fe2+ salts for two hours prior to analytical gel-filtration using a Superdex 200 PC 3.2/30 column (GE Healthcare).	FIG
+5	9	Fe2+	chemical	Both Fe2+ salts tested induced the formation of decamer indicated by the peak between 1.2 and 1.6 ml.	FIG
+48	55	decamer	oligomeric_state	Both Fe2+ salts tested induced the formation of decamer indicated by the peak between 1.2 and 1.6 ml.	FIG
+0	9	Monomeric	oligomeric_state	Monomeric and decameric samples of EncFtnsH are shown as controls.	FIG
+14	23	decameric	oligomeric_state	Monomeric and decameric samples of EncFtnsH are shown as controls.	FIG
+35	43	EncFtnsH	protein	Monomeric and decameric samples of EncFtnsH are shown as controls.	FIG
+0	5	Peaks	evidence	Peaks around 0.8 ml were seen as protein aggregation.	FIG
+4	29	Analytical gel filtration	experimental_method	(C) Analytical gel filtration of EncFtn monomer at different concentrations to illustrate the effect of protein concentration on multimerization.	FIG
+33	39	EncFtn	protein	(C) Analytical gel filtration of EncFtn monomer at different concentrations to illustrate the effect of protein concentration on multimerization.	FIG
+40	47	monomer	oligomeric_state	(C) Analytical gel filtration of EncFtn monomer at different concentrations to illustrate the effect of protein concentration on multimerization.	FIG
+39	44	dimer	oligomeric_state	The major peak shows a shift towards a dimer species at high concentration of protein, but the ratio of this peak (1.5–1.8 ml) to the decamer peak (1.2–1.5 ml) does not change when compared to the low concentration sample.	FIG
+134	141	decamer	oligomeric_state	The major peak shows a shift towards a dimer species at high concentration of protein, but the ratio of this peak (1.5–1.8 ml) to the decamer peak (1.2–1.5 ml) does not change when compared to the low concentration sample.	FIG
+0	14	Gel-filtration	experimental_method	Gel-filtration peak area ratios for EncFtnsH decamer and monomer on addition of different metal ions.	TABLE
+15	31	peak area ratios	evidence	Gel-filtration peak area ratios for EncFtnsH decamer and monomer on addition of different metal ions.	TABLE
+36	44	EncFtnsH	protein	Gel-filtration peak area ratios for EncFtnsH decamer and monomer on addition of different metal ions.	TABLE
+45	52	decamer	oligomeric_state	Gel-filtration peak area ratios for EncFtnsH decamer and monomer on addition of different metal ions.	TABLE
+57	64	monomer	oligomeric_state	Gel-filtration peak area ratios for EncFtnsH decamer and monomer on addition of different metal ions.	TABLE
+0	8	EncFtnsH	protein	EncFtnsH was produced in E. coli BL21(DE3) cultured in MM and MM with 1 mM Fe(NH4)2(SO4)2 (MM+Fe2+) and purified by gel-filtration chromatography using an Superdex 200 16/60 column (GE Healthcare).	TABLE
+25	42	E. coli BL21(DE3)	species	EncFtnsH was produced in E. coli BL21(DE3) cultured in MM and MM with 1 mM Fe(NH4)2(SO4)2 (MM+Fe2+) and purified by gel-filtration chromatography using an Superdex 200 16/60 column (GE Healthcare).	TABLE
+55	57	MM	experimental_method	EncFtnsH was produced in E. coli BL21(DE3) cultured in MM and MM with 1 mM Fe(NH4)2(SO4)2 (MM+Fe2+) and purified by gel-filtration chromatography using an Superdex 200 16/60 column (GE Healthcare).	TABLE
+62	64	MM	experimental_method	EncFtnsH was produced in E. coli BL21(DE3) cultured in MM and MM with 1 mM Fe(NH4)2(SO4)2 (MM+Fe2+) and purified by gel-filtration chromatography using an Superdex 200 16/60 column (GE Healthcare).	TABLE
+75	89	Fe(NH4)2(SO4)2	chemical	EncFtnsH was produced in E. coli BL21(DE3) cultured in MM and MM with 1 mM Fe(NH4)2(SO4)2 (MM+Fe2+) and purified by gel-filtration chromatography using an Superdex 200 16/60 column (GE Healthcare).	TABLE
+91	93	MM	experimental_method	EncFtnsH was produced in E. coli BL21(DE3) cultured in MM and MM with 1 mM Fe(NH4)2(SO4)2 (MM+Fe2+) and purified by gel-filtration chromatography using an Superdex 200 16/60 column (GE Healthcare).	TABLE
+94	98	Fe2+	chemical	EncFtnsH was produced in E. coli BL21(DE3) cultured in MM and MM with 1 mM Fe(NH4)2(SO4)2 (MM+Fe2+) and purified by gel-filtration chromatography using an Superdex 200 16/60 column (GE Healthcare).	TABLE
+116	145	gel-filtration chromatography	experimental_method	EncFtnsH was produced in E. coli BL21(DE3) cultured in MM and MM with 1 mM Fe(NH4)2(SO4)2 (MM+Fe2+) and purified by gel-filtration chromatography using an Superdex 200 16/60 column (GE Healthcare).	TABLE
+0	7	Monomer	oligomeric_state	Monomer fractions of EncFtnsH purified from MM were pooled and run in subsequent analytical gel-filtration runs over the course of three days.	TABLE
+21	29	EncFtnsH	protein	Monomer fractions of EncFtnsH purified from MM were pooled and run in subsequent analytical gel-filtration runs over the course of three days.	TABLE
+44	46	MM	experimental_method	Monomer fractions of EncFtnsH purified from MM were pooled and run in subsequent analytical gel-filtration runs over the course of three days.	TABLE
+81	106	analytical gel-filtration	experimental_method	Monomer fractions of EncFtnsH purified from MM were pooled and run in subsequent analytical gel-filtration runs over the course of three days.	TABLE
+11	19	EncFtnsH	protein	Samples of EncFtnsH monomer were incubated with one molar equivalent of metal ion salts at room temperature for two hours before analysis by analytical gel filtration chromatography (AGF) using a Superdex 200 10/300 GL column.	TABLE
+20	27	monomer	oligomeric_state	Samples of EncFtnsH monomer were incubated with one molar equivalent of metal ion salts at room temperature for two hours before analysis by analytical gel filtration chromatography (AGF) using a Superdex 200 10/300 GL column.	TABLE
+141	181	analytical gel filtration chromatography	experimental_method	Samples of EncFtnsH monomer were incubated with one molar equivalent of metal ion salts at room temperature for two hours before analysis by analytical gel filtration chromatography (AGF) using a Superdex 200 10/300 GL column.	TABLE
+183	186	AGF	experimental_method	Samples of EncFtnsH monomer were incubated with one molar equivalent of metal ion salts at room temperature for two hours before analysis by analytical gel filtration chromatography (AGF) using a Superdex 200 10/300 GL column.	TABLE
+31	36	peaks	evidence	The area for resulting protein peaks were calculated using the Unicorn software (GE Healthcare); peak ratios were calculated to quantify the propensity of EncFtnsH to multimerize in the presence of the different metal ions.	TABLE
+97	108	peak ratios	evidence	The area for resulting protein peaks were calculated using the Unicorn software (GE Healthcare); peak ratios were calculated to quantify the propensity of EncFtnsH to multimerize in the presence of the different metal ions.	TABLE
+155	163	EncFtnsH	protein	The area for resulting protein peaks were calculated using the Unicorn software (GE Healthcare); peak ratios were calculated to quantify the propensity of EncFtnsH to multimerize in the presence of the different metal ions.	TABLE
+186	197	presence of	protein_state	The area for resulting protein peaks were calculated using the Unicorn software (GE Healthcare); peak ratios were calculated to quantify the propensity of EncFtnsH to multimerize in the presence of the different metal ions.	TABLE
+28	35	monomer	oligomeric_state	The change in the ratios of monomer to decamer over the three days of experiments may be a consequence of experimental variability, or the propensity of this protein to equilibrate towards decamer over time.	TABLE
+39	46	decamer	oligomeric_state	The change in the ratios of monomer to decamer over the three days of experiments may be a consequence of experimental variability, or the propensity of this protein to equilibrate towards decamer over time.	TABLE
+189	196	decamer	oligomeric_state	The change in the ratios of monomer to decamer over the three days of experiments may be a consequence of experimental variability, or the propensity of this protein to equilibrate towards decamer over time.	TABLE
+14	21	decamer	oligomeric_state	The increased decamer: monomer ratio seen in the presence of Fe2+, Co2+, and Zn2+ indicates that these metal ions facilitate multimerization of the EncFtnsH protein, while the other metal ions tested do not appear to induce multimerization.	TABLE
+23	30	monomer	oligomeric_state	The increased decamer: monomer ratio seen in the presence of Fe2+, Co2+, and Zn2+ indicates that these metal ions facilitate multimerization of the EncFtnsH protein, while the other metal ions tested do not appear to induce multimerization.	TABLE
+49	60	presence of	protein_state	The increased decamer: monomer ratio seen in the presence of Fe2+, Co2+, and Zn2+ indicates that these metal ions facilitate multimerization of the EncFtnsH protein, while the other metal ions tested do not appear to induce multimerization.	TABLE
+61	65	Fe2+	chemical	The increased decamer: monomer ratio seen in the presence of Fe2+, Co2+, and Zn2+ indicates that these metal ions facilitate multimerization of the EncFtnsH protein, while the other metal ions tested do not appear to induce multimerization.	TABLE
+67	71	Co2+	chemical	The increased decamer: monomer ratio seen in the presence of Fe2+, Co2+, and Zn2+ indicates that these metal ions facilitate multimerization of the EncFtnsH protein, while the other metal ions tested do not appear to induce multimerization.	TABLE
+77	81	Zn2+	chemical	The increased decamer: monomer ratio seen in the presence of Fe2+, Co2+, and Zn2+ indicates that these metal ions facilitate multimerization of the EncFtnsH protein, while the other metal ions tested do not appear to induce multimerization.	TABLE
+148	156	EncFtnsH	protein	The increased decamer: monomer ratio seen in the presence of Fe2+, Co2+, and Zn2+ indicates that these metal ions facilitate multimerization of the EncFtnsH protein, while the other metal ions tested do not appear to induce multimerization.	TABLE
+4	29	analytical gel filtration	experimental_method	The analytical gel filtration experiment was repeated twice using two independent preparations of protein, of which values calculated from one sample are presented here.	TABLE
+14	21	Monomer	oligomeric_state	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+27	34	Decamer	oligomeric_state	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+40	47	Decamer	oligomeric_state	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+48	55	Monomer	oligomeric_state	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+58	72	Gel filtration	experimental_method	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+101	109	EncFtnsH	protein	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+110	112	MM	experimental_method	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+130	138	EncFtnsH	protein	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+139	141	MM	experimental_method	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+142	146	Fe2+	chemical	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+166	191	Analytical Gel filtration	experimental_method	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+197	205	EncFtnsH	protein	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+206	213	decamer	oligomeric_state	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+240	248	EncFtnsH	protein	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+249	256	monomer	oligomeric_state	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+282	296	Fe(NH4)2(SO4)2	chemical	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+297	305	EncFtnsH	protein	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+306	313	monomer	oligomeric_state	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+330	339	FeSO4-HCl	chemical	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+340	348	EncFtnsH	protein	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+349	356	monomer	oligomeric_state	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+373	398	Analytical Gel filtration	experimental_method	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+404	412	EncFtnsH	protein	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+413	420	monomer	oligomeric_state	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+446	451	CoCl2	chemical	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+452	460	EncFtnsH	protein	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+461	468	monomer	oligomeric_state	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+485	490	MnCl2	chemical	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+491	499	EncFtnsH	protein	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+500	507	monomer	oligomeric_state	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+523	528	ZnSO4	chemical	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+529	537	EncFtnsH	protein	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+538	545	monomer	oligomeric_state	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+561	566	FeCl3	chemical	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+567	575	EncFtnsH	protein	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+576	583	monomer	oligomeric_state	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+599	624	Analytical Gel filtration	experimental_method	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+630	638	EncFtnsH	protein	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+639	646	monomer	oligomeric_state	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+672	677	MgSO4	chemical	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+678	686	EncFtnsH	protein	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+687	694	monomer	oligomeric_state	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+710	720	Ca acetate	chemical	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+721	729	EncFtnsH	protein	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+730	737	monomer	oligomeric_state	"Method	Sample	Monomer area	Decamer area	Decamer/Monomer	 	Gel filtration Superdex 200 chromatography	EncFtnsH-MM	64.3	583.6	0.1	 	EncFtnsH-MM+Fe2+	1938.4	426.4	4.5	 	Analytical Gel filtration Day1	EncFtnsH-decamer fractions	20.2	1.8	11.2	 	EncFtnsH-monomer fractions	2.9	21.9	0.1	 	Fe(NH4)2(SO4)2/EncFtnsH-monomer	11.0	13.0	0.8	 	FeSO4-HCl/EncFtnsH-monomer	11.3	11.4	1.0	 	Analytical Gel filtration Day2	EncFtnsH-monomer fractions	8.3	22.8	0.4	 	CoCl2/EncFtnsH-monomer	17.7	14.5	1.2	 	MnCl2/EncFtnsH-monomer	3.1	30.5	0.1	 	ZnSO4/EncFtnsH-monomer	20.4	9.0	2.3	 	FeCl3/EncFtnsH-monomer	3.9	28.6	0.1	 	Analytical Gel filtration Day3	EncFtnsH-monomer fractions	6.3	23.4	0.3	 	MgSO4/EncFtnsH-monomer	5.8	30.2	0.2	 	Ca acetate/EncFtnsH-monomer	5.6	25.2	0.2	 	"	TABLE
+12	20	EncFtnsH	protein	We purified EncFtnsH from E. coli grown in MM with or without the addition of 1 mM Fe(NH4)2(SO4)2.	RESULTS
+26	33	E. coli	species	We purified EncFtnsH from E. coli grown in MM with or without the addition of 1 mM Fe(NH4)2(SO4)2.	RESULTS
+43	45	MM	experimental_method	We purified EncFtnsH from E. coli grown in MM with or without the addition of 1 mM Fe(NH4)2(SO4)2.	RESULTS
+83	97	Fe(NH4)2(SO4)2	chemical	We purified EncFtnsH from E. coli grown in MM with or without the addition of 1 mM Fe(NH4)2(SO4)2.	RESULTS
+4	11	decamer	oligomeric_state	The decamer to monomer ratio in the sample purified from cells grown in iron-supplemented media was 4.5, while that from the iron-free media was 0.11, suggesting that iron induces the oligomerization of EncFtnsH in vivo (Figure 3A, Table 3).	RESULTS
+15	22	monomer	oligomeric_state	The decamer to monomer ratio in the sample purified from cells grown in iron-supplemented media was 4.5, while that from the iron-free media was 0.11, suggesting that iron induces the oligomerization of EncFtnsH in vivo (Figure 3A, Table 3).	RESULTS
+72	76	iron	chemical	The decamer to monomer ratio in the sample purified from cells grown in iron-supplemented media was 4.5, while that from the iron-free media was 0.11, suggesting that iron induces the oligomerization of EncFtnsH in vivo (Figure 3A, Table 3).	RESULTS
+125	134	iron-free	protein_state	The decamer to monomer ratio in the sample purified from cells grown in iron-supplemented media was 4.5, while that from the iron-free media was 0.11, suggesting that iron induces the oligomerization of EncFtnsH in vivo (Figure 3A, Table 3).	RESULTS
+167	171	iron	chemical	The decamer to monomer ratio in the sample purified from cells grown in iron-supplemented media was 4.5, while that from the iron-free media was 0.11, suggesting that iron induces the oligomerization of EncFtnsH in vivo (Figure 3A, Table 3).	RESULTS
+203	211	EncFtnsH	protein	The decamer to monomer ratio in the sample purified from cells grown in iron-supplemented media was 4.5, while that from the iron-free media was 0.11, suggesting that iron induces the oligomerization of EncFtnsH in vivo (Figure 3A, Table 3).	RESULTS
+47	55	EncFtnsH	protein	To test the metal-dependent oligomerization of EncFtnsH in vitro, we incubated the protein with various metal cations and subjected samples to analytical SEC and non-denaturing PAGE.	RESULTS
+69	78	incubated	experimental_method	To test the metal-dependent oligomerization of EncFtnsH in vitro, we incubated the protein with various metal cations and subjected samples to analytical SEC and non-denaturing PAGE.	RESULTS
+143	157	analytical SEC	experimental_method	To test the metal-dependent oligomerization of EncFtnsH in vitro, we incubated the protein with various metal cations and subjected samples to analytical SEC and non-denaturing PAGE.	RESULTS
+162	181	non-denaturing PAGE	experimental_method	To test the metal-dependent oligomerization of EncFtnsH in vitro, we incubated the protein with various metal cations and subjected samples to analytical SEC and non-denaturing PAGE.	RESULTS
+27	32	Fe2+,	chemical	Of the metals tested, only Fe2+, Zn2+ and Co2+ induced the formation of significant amounts of the decamer (Figure 3B, Figure 3—figure supplement 1/2).	RESULTS
+33	37	Zn2+	chemical	Of the metals tested, only Fe2+, Zn2+ and Co2+ induced the formation of significant amounts of the decamer (Figure 3B, Figure 3—figure supplement 1/2).	RESULTS
+42	46	Co2+	chemical	Of the metals tested, only Fe2+, Zn2+ and Co2+ induced the formation of significant amounts of the decamer (Figure 3B, Figure 3—figure supplement 1/2).	RESULTS
+99	106	decamer	oligomeric_state	Of the metals tested, only Fe2+, Zn2+ and Co2+ induced the formation of significant amounts of the decamer (Figure 3B, Figure 3—figure supplement 1/2).	RESULTS
+6	10	Fe2+	chemical	While Fe2+ induces the multimerization of EncFtnsH, Fe3+ in the form of FeCl3 does not have this effect on the protein, highlighting the apparent preference this protein has for the ferrous form of iron.	RESULTS
+42	50	EncFtnsH	protein	While Fe2+ induces the multimerization of EncFtnsH, Fe3+ in the form of FeCl3 does not have this effect on the protein, highlighting the apparent preference this protein has for the ferrous form of iron.	RESULTS
+52	56	Fe3+	chemical	While Fe2+ induces the multimerization of EncFtnsH, Fe3+ in the form of FeCl3 does not have this effect on the protein, highlighting the apparent preference this protein has for the ferrous form of iron.	RESULTS
+72	77	FeCl3	chemical	While Fe2+ induces the multimerization of EncFtnsH, Fe3+ in the form of FeCl3 does not have this effect on the protein, highlighting the apparent preference this protein has for the ferrous form of iron.	RESULTS
+182	202	ferrous form of iron	chemical	While Fe2+ induces the multimerization of EncFtnsH, Fe3+ in the form of FeCl3 does not have this effect on the protein, highlighting the apparent preference this protein has for the ferrous form of iron.	RESULTS
+39	47	EncFtnsH	protein	To determine if the oligomerization of EncFtnsH was concentration dependent we performed analytical SEC at 90 and 700 µM protein concentration (Figure 3C).	RESULTS
+89	103	analytical SEC	experimental_method	To determine if the oligomerization of EncFtnsH was concentration dependent we performed analytical SEC at 90 and 700 µM protein concentration (Figure 3C).	RESULTS
+48	57	decameric	oligomeric_state	At the higher concentration, no increase in the decameric form of EncFtn was observed; however, the shift in the major peak from the position of the monomer species indicated a tendency to dimerize at high concentration.	RESULTS
+66	72	EncFtn	protein	At the higher concentration, no increase in the decameric form of EncFtn was observed; however, the shift in the major peak from the position of the monomer species indicated a tendency to dimerize at high concentration.	RESULTS
+149	156	monomer	oligomeric_state	At the higher concentration, no increase in the decameric form of EncFtn was observed; however, the shift in the major peak from the position of the monomer species indicated a tendency to dimerize at high concentration.	RESULTS
+189	197	dimerize	oligomeric_state	At the higher concentration, no increase in the decameric form of EncFtn was observed; however, the shift in the major peak from the position of the monomer species indicated a tendency to dimerize at high concentration.	RESULTS
+0	17	Crystal structure	evidence	Crystal structure of EncFtnsH	RESULTS
+21	29	EncFtnsH	protein	Crystal structure of EncFtnsH	RESULTS
+25	33	EncFtnsH	protein	Electrostatic surface of EncFtnsH.	FIG
+34	42	EncFtnsH	protein	The solvent accessible surface of EncFtnsH is shown, colored by electrostatic potential as calculated using the APBS plugin in PyMOL.	FIG
+129	137	EncFtnsH	protein	Negatively charged regions are colored red and positive regions in blue, neutral regions in grey. (A) View of the surface of the EncFtnsH decamer looking down the central axis.	FIG
+138	145	decamer	oligomeric_state	Negatively charged regions are colored red and positive regions in blue, neutral regions in grey. (A) View of the surface of the EncFtnsH decamer looking down the central axis.	FIG
+95	109	central cavity	site	(B) Orthogonal view of (A). (C) Cutaway view of (B) showing the charge distribution within the central cavity.	FIG
+0	17	Crystal structure	evidence	Crystal structure of EncFtnsH.	FIG
+21	29	EncFtnsH	protein	Crystal structure of EncFtnsH.	FIG
+28	36	EncFtnsH	protein	(A) Overall architecture of EncFtnsH. Transparent solvent accessible surface view with α-helices shown as tubes and bound metal ions as spheres.	FIG
+87	96	α-helices	structure_element	(A) Overall architecture of EncFtnsH. Transparent solvent accessible surface view with α-helices shown as tubes and bound metal ions as spheres.	FIG
+12	20	subunits	structure_element	Alternating subunits are colored blue and green for clarity.	FIG
+4	17	doughnut-like	structure_element	The doughnut-like decamer is 7 nm in diameter and 4.5 nm thick. (B) Monomer of EncFtnsH shown as a secondary structure cartoon. (C/D) Dimer interfaces formed in the decameric ring of EncFtnsH. Subunits are shown as secondary structure cartoons and colored blue and green for clarity.	FIG
+18	25	decamer	oligomeric_state	The doughnut-like decamer is 7 nm in diameter and 4.5 nm thick. (B) Monomer of EncFtnsH shown as a secondary structure cartoon. (C/D) Dimer interfaces formed in the decameric ring of EncFtnsH. Subunits are shown as secondary structure cartoons and colored blue and green for clarity.	FIG
+68	75	Monomer	oligomeric_state	The doughnut-like decamer is 7 nm in diameter and 4.5 nm thick. (B) Monomer of EncFtnsH shown as a secondary structure cartoon. (C/D) Dimer interfaces formed in the decameric ring of EncFtnsH. Subunits are shown as secondary structure cartoons and colored blue and green for clarity.	FIG
+79	87	EncFtnsH	protein	The doughnut-like decamer is 7 nm in diameter and 4.5 nm thick. (B) Monomer of EncFtnsH shown as a secondary structure cartoon. (C/D) Dimer interfaces formed in the decameric ring of EncFtnsH. Subunits are shown as secondary structure cartoons and colored blue and green for clarity.	FIG
+134	150	Dimer interfaces	site	The doughnut-like decamer is 7 nm in diameter and 4.5 nm thick. (B) Monomer of EncFtnsH shown as a secondary structure cartoon. (C/D) Dimer interfaces formed in the decameric ring of EncFtnsH. Subunits are shown as secondary structure cartoons and colored blue and green for clarity.	FIG
+165	174	decameric	oligomeric_state	The doughnut-like decamer is 7 nm in diameter and 4.5 nm thick. (B) Monomer of EncFtnsH shown as a secondary structure cartoon. (C/D) Dimer interfaces formed in the decameric ring of EncFtnsH. Subunits are shown as secondary structure cartoons and colored blue and green for clarity.	FIG
+175	179	ring	structure_element	The doughnut-like decamer is 7 nm in diameter and 4.5 nm thick. (B) Monomer of EncFtnsH shown as a secondary structure cartoon. (C/D) Dimer interfaces formed in the decameric ring of EncFtnsH. Subunits are shown as secondary structure cartoons and colored blue and green for clarity.	FIG
+183	191	EncFtnsH	protein	The doughnut-like decamer is 7 nm in diameter and 4.5 nm thick. (B) Monomer of EncFtnsH shown as a secondary structure cartoon. (C/D) Dimer interfaces formed in the decameric ring of EncFtnsH. Subunits are shown as secondary structure cartoons and colored blue and green for clarity.	FIG
+193	201	Subunits	structure_element	The doughnut-like decamer is 7 nm in diameter and 4.5 nm thick. (B) Monomer of EncFtnsH shown as a secondary structure cartoon. (C/D) Dimer interfaces formed in the decameric ring of EncFtnsH. Subunits are shown as secondary structure cartoons and colored blue and green for clarity.	FIG
+49	53	Fe3+	chemical	Bound metal ions are shown as orange spheres for Fe3+ and grey and white spheres for Ca2+.	FIG
+85	89	Ca2+	chemical	Bound metal ions are shown as orange spheres for Fe3+ and grey and white spheres for Ca2+.	FIG
+18	35	crystal structure	evidence	We determined the crystal structure of EncFtnsH by molecular replacement to 2.0 Å resolution (see Table 1 for X-ray data collection and refinement statistics).	RESULTS
+39	47	EncFtnsH	protein	We determined the crystal structure of EncFtnsH by molecular replacement to 2.0 Å resolution (see Table 1 for X-ray data collection and refinement statistics).	RESULTS
+51	72	molecular replacement	experimental_method	We determined the crystal structure of EncFtnsH by molecular replacement to 2.0 Å resolution (see Table 1 for X-ray data collection and refinement statistics).	RESULTS
+110	157	X-ray data collection and refinement statistics	evidence	We determined the crystal structure of EncFtnsH by molecular replacement to 2.0 Å resolution (see Table 1 for X-ray data collection and refinement statistics).	RESULTS
+54	62	monomers	oligomeric_state	The crystallographic asymmetric unit contained thirty monomers of EncFtn with visible electron density for residues 7 – 96 in each chain.	RESULTS
+66	72	EncFtn	protein	The crystallographic asymmetric unit contained thirty monomers of EncFtn with visible electron density for residues 7 – 96 in each chain.	RESULTS
+86	102	electron density	evidence	The crystallographic asymmetric unit contained thirty monomers of EncFtn with visible electron density for residues 7 – 96 in each chain.	RESULTS
+116	122	7 – 96	residue_range	The crystallographic asymmetric unit contained thirty monomers of EncFtn with visible electron density for residues 7 – 96 in each chain.	RESULTS
+52	59	annular	structure_element	The protein chains were arranged as three identical annular decamers, each with D5 symmetry.	RESULTS
+60	68	decamers	oligomeric_state	The protein chains were arranged as three identical annular decamers, each with D5 symmetry.	RESULTS
+4	11	decamer	oligomeric_state	The decamer has a diameter of 7 nm and thickness of 4 nm (Figure 4A).	RESULTS
+4	11	monomer	oligomeric_state	The monomer of EncFtn has an N-terminal 310-helix that precedes two 4 nm long antiparallel α-helices arranged with their long axes at 25° to each other; these helices are followed by a shorter 1.4 nm helix projecting at 70° from α2 (Figure 4B).	RESULTS
+15	21	EncFtn	protein	The monomer of EncFtn has an N-terminal 310-helix that precedes two 4 nm long antiparallel α-helices arranged with their long axes at 25° to each other; these helices are followed by a shorter 1.4 nm helix projecting at 70° from α2 (Figure 4B).	RESULTS
+40	49	310-helix	structure_element	The monomer of EncFtn has an N-terminal 310-helix that precedes two 4 nm long antiparallel α-helices arranged with their long axes at 25° to each other; these helices are followed by a shorter 1.4 nm helix projecting at 70° from α2 (Figure 4B).	RESULTS
+78	100	antiparallel α-helices	structure_element	The monomer of EncFtn has an N-terminal 310-helix that precedes two 4 nm long antiparallel α-helices arranged with their long axes at 25° to each other; these helices are followed by a shorter 1.4 nm helix projecting at 70° from α2 (Figure 4B).	RESULTS
+159	166	helices	structure_element	The monomer of EncFtn has an N-terminal 310-helix that precedes two 4 nm long antiparallel α-helices arranged with their long axes at 25° to each other; these helices are followed by a shorter 1.4 nm helix projecting at 70° from α2 (Figure 4B).	RESULTS
+200	205	helix	structure_element	The monomer of EncFtn has an N-terminal 310-helix that precedes two 4 nm long antiparallel α-helices arranged with their long axes at 25° to each other; these helices are followed by a shorter 1.4 nm helix projecting at 70° from α2 (Figure 4B).	RESULTS
+229	231	α2	structure_element	The monomer of EncFtn has an N-terminal 310-helix that precedes two 4 nm long antiparallel α-helices arranged with their long axes at 25° to each other; these helices are followed by a shorter 1.4 nm helix projecting at 70° from α2 (Figure 4B).	RESULTS
+4	21	C-terminal region	structure_element	The C-terminal region of the crystallized construct extends from the outer circumference of the ring, indicating that the encapsulin localization sequence in the full-length protein is on the exterior of the ring and is thus free to interact with its binding site on the encapsulin shell protein.	RESULTS
+96	100	ring	structure_element	The C-terminal region of the crystallized construct extends from the outer circumference of the ring, indicating that the encapsulin localization sequence in the full-length protein is on the exterior of the ring and is thus free to interact with its binding site on the encapsulin shell protein.	RESULTS
+122	154	encapsulin localization sequence	site	The C-terminal region of the crystallized construct extends from the outer circumference of the ring, indicating that the encapsulin localization sequence in the full-length protein is on the exterior of the ring and is thus free to interact with its binding site on the encapsulin shell protein.	RESULTS
+162	173	full-length	protein_state	The C-terminal region of the crystallized construct extends from the outer circumference of the ring, indicating that the encapsulin localization sequence in the full-length protein is on the exterior of the ring and is thus free to interact with its binding site on the encapsulin shell protein.	RESULTS
+208	212	ring	structure_element	The C-terminal region of the crystallized construct extends from the outer circumference of the ring, indicating that the encapsulin localization sequence in the full-length protein is on the exterior of the ring and is thus free to interact with its binding site on the encapsulin shell protein.	RESULTS
+251	263	binding site	site	The C-terminal region of the crystallized construct extends from the outer circumference of the ring, indicating that the encapsulin localization sequence in the full-length protein is on the exterior of the ring and is thus free to interact with its binding site on the encapsulin shell protein.	RESULTS
+271	281	encapsulin	protein	The C-terminal region of the crystallized construct extends from the outer circumference of the ring, indicating that the encapsulin localization sequence in the full-length protein is on the exterior of the ring and is thus free to interact with its binding site on the encapsulin shell protein.	RESULTS
+282	287	shell	structure_element	The C-terminal region of the crystallized construct extends from the outer circumference of the ring, indicating that the encapsulin localization sequence in the full-length protein is on the exterior of the ring and is thus free to interact with its binding site on the encapsulin shell protein.	RESULTS
+4	11	monomer	oligomeric_state	The monomer of EncFtnsH forms two distinct dimer interfaces within the decamer (Figure 4 C/D).	RESULTS
+15	23	EncFtnsH	protein	The monomer of EncFtnsH forms two distinct dimer interfaces within the decamer (Figure 4 C/D).	RESULTS
+43	59	dimer interfaces	site	The monomer of EncFtnsH forms two distinct dimer interfaces within the decamer (Figure 4 C/D).	RESULTS
+71	78	decamer	oligomeric_state	The monomer of EncFtnsH forms two distinct dimer interfaces within the decamer (Figure 4 C/D).	RESULTS
+10	15	dimer	oligomeric_state	The first dimer is formed from two monomers arranged antiparallel to each other, with α1 from each monomer interacting along their lengths and α3 interdigitating with α2 and α3 of the partner chain.	RESULTS
+35	43	monomers	oligomeric_state	The first dimer is formed from two monomers arranged antiparallel to each other, with α1 from each monomer interacting along their lengths and α3 interdigitating with α2 and α3 of the partner chain.	RESULTS
+86	88	α1	structure_element	The first dimer is formed from two monomers arranged antiparallel to each other, with α1 from each monomer interacting along their lengths and α3 interdigitating with α2 and α3 of the partner chain.	RESULTS
+99	106	monomer	oligomeric_state	The first dimer is formed from two monomers arranged antiparallel to each other, with α1 from each monomer interacting along their lengths and α3 interdigitating with α2 and α3 of the partner chain.	RESULTS
+143	145	α3	structure_element	The first dimer is formed from two monomers arranged antiparallel to each other, with α1 from each monomer interacting along their lengths and α3 interdigitating with α2 and α3 of the partner chain.	RESULTS
+167	169	α2	structure_element	The first dimer is formed from two monomers arranged antiparallel to each other, with α1 from each monomer interacting along their lengths and α3 interdigitating with α2 and α3 of the partner chain.	RESULTS
+174	176	α3	structure_element	The first dimer is formed from two monomers arranged antiparallel to each other, with α1 from each monomer interacting along their lengths and α3 interdigitating with α2 and α3 of the partner chain.	RESULTS
+5	14	interface	site	This interface buries one third of the surface area from each partner and is stabilized by thirty hydrogen bonds and fourteen salt bridges (Figure 4C).	RESULTS
+98	112	hydrogen bonds	bond_interaction	This interface buries one third of the surface area from each partner and is stabilized by thirty hydrogen bonds and fourteen salt bridges (Figure 4C).	RESULTS
+126	138	salt bridges	bond_interaction	This interface buries one third of the surface area from each partner and is stabilized by thirty hydrogen bonds and fourteen salt bridges (Figure 4C).	RESULTS
+11	26	dimer interface	site	The second dimer interface forms an antiparallel four-helix bundle between helices 1 and 2 from each monomer (Figure 4D).	RESULTS
+36	66	antiparallel four-helix bundle	structure_element	The second dimer interface forms an antiparallel four-helix bundle between helices 1 and 2 from each monomer (Figure 4D).	RESULTS
+75	90	helices 1 and 2	structure_element	The second dimer interface forms an antiparallel four-helix bundle between helices 1 and 2 from each monomer (Figure 4D).	RESULTS
+101	108	monomer	oligomeric_state	The second dimer interface forms an antiparallel four-helix bundle between helices 1 and 2 from each monomer (Figure 4D).	RESULTS
+5	14	interface	site	This interface is less extensive than the first and is stabilized by twenty-one hydrogen bonds, six salt bridges, and a number of metal ions.	RESULTS
+80	94	hydrogen bonds	bond_interaction	This interface is less extensive than the first and is stabilized by twenty-one hydrogen bonds, six salt bridges, and a number of metal ions.	RESULTS
+100	112	salt bridges	bond_interaction	This interface is less extensive than the first and is stabilized by twenty-one hydrogen bonds, six salt bridges, and a number of metal ions.	RESULTS
+23	31	monomers	oligomeric_state	The arrangement of ten monomers in alternating orientation forms the decamer of EncFtn, which assembles as a pentamer of dimers (Figure 4A).	RESULTS
+69	76	decamer	oligomeric_state	The arrangement of ten monomers in alternating orientation forms the decamer of EncFtn, which assembles as a pentamer of dimers (Figure 4A).	RESULTS
+80	86	EncFtn	protein	The arrangement of ten monomers in alternating orientation forms the decamer of EncFtn, which assembles as a pentamer of dimers (Figure 4A).	RESULTS
+109	117	pentamer	oligomeric_state	The arrangement of ten monomers in alternating orientation forms the decamer of EncFtn, which assembles as a pentamer of dimers (Figure 4A).	RESULTS
+121	127	dimers	oligomeric_state	The arrangement of ten monomers in alternating orientation forms the decamer of EncFtn, which assembles as a pentamer of dimers (Figure 4A).	RESULTS
+5	12	monomer	oligomeric_state	Each monomer lies at 45° relative to the vertical central-axis of the ring, with the N-termini of alternating subunits capping the center of the ring at each end, while the C-termini are arranged around the circumference.	RESULTS
+70	74	ring	structure_element	Each monomer lies at 45° relative to the vertical central-axis of the ring, with the N-termini of alternating subunits capping the center of the ring at each end, while the C-termini are arranged around the circumference.	RESULTS
+110	118	subunits	structure_element	Each monomer lies at 45° relative to the vertical central-axis of the ring, with the N-termini of alternating subunits capping the center of the ring at each end, while the C-termini are arranged around the circumference.	RESULTS
+145	149	ring	structure_element	Each monomer lies at 45° relative to the vertical central-axis of the ring, with the N-termini of alternating subunits capping the center of the ring at each end, while the C-termini are arranged around the circumference.	RESULTS
+4	16	central hole	site	The central hole in the ring is 2.5 nm at its widest in the center of the complex, and 1.5 nm at its narrowest point near the outer surface, although it should be noted that a number of residues at the N-terminus are not visible in the crystallographic electron density and these may occupy the central channel.	RESULTS
+24	28	ring	structure_element	The central hole in the ring is 2.5 nm at its widest in the center of the complex, and 1.5 nm at its narrowest point near the outer surface, although it should be noted that a number of residues at the N-terminus are not visible in the crystallographic electron density and these may occupy the central channel.	RESULTS
+236	269	crystallographic electron density	evidence	The central hole in the ring is 2.5 nm at its widest in the center of the complex, and 1.5 nm at its narrowest point near the outer surface, although it should be noted that a number of residues at the N-terminus are not visible in the crystallographic electron density and these may occupy the central channel.	RESULTS
+295	310	central channel	site	The central hole in the ring is 2.5 nm at its widest in the center of the complex, and 1.5 nm at its narrowest point near the outer surface, although it should be noted that a number of residues at the N-terminus are not visible in the crystallographic electron density and these may occupy the central channel.	RESULTS
+19	26	decamer	oligomeric_state	The surface of the decamer has distinct negatively charged patches, both within the central hole and on the outer circumference, which form spokes through the radius of the complex (Figure 4—figure supplement 1).	RESULTS
+40	66	negatively charged patches	site	The surface of the decamer has distinct negatively charged patches, both within the central hole and on the outer circumference, which form spokes through the radius of the complex (Figure 4—figure supplement 1).	RESULTS
+84	96	central hole	site	The surface of the decamer has distinct negatively charged patches, both within the central hole and on the outer circumference, which form spokes through the radius of the complex (Figure 4—figure supplement 1).	RESULTS
+140	146	spokes	structure_element	The surface of the decamer has distinct negatively charged patches, both within the central hole and on the outer circumference, which form spokes through the radius of the complex (Figure 4—figure supplement 1).	RESULTS
+0	6	EncFtn	protein	EncFtn ferroxidase center	RESULTS
+7	25	ferroxidase center	site	EncFtn ferroxidase center	RESULTS
+9	28	ligand-binding site	site	Putative ligand-binding site in EncFtnsH.	FIG
+32	40	EncFtnsH	protein	Putative ligand-binding site in EncFtnsH.	FIG
+33	48	dimer interface	site	(A) Wall-eyed stereo view of the dimer interface of EncFtn.	FIG
+52	58	EncFtn	protein	(A) Wall-eyed stereo view of the dimer interface of EncFtn.	FIG
+41	66	2mFo-DFc electron density	evidence	Protein chains are shown as sticks, with 2mFo-DFc electron density shown in blue mesh and contoured at 1.5 σ and mFo-DFc shown in green mesh and contoured at 3 σ. (B) Wall-eyed stereo view of putative metal binding site at the external surface of EncFtnsH. Protein chains and electron density maps are shown as in (A).	FIG
+113	120	mFo-DFc	evidence	Protein chains are shown as sticks, with 2mFo-DFc electron density shown in blue mesh and contoured at 1.5 σ and mFo-DFc shown in green mesh and contoured at 3 σ. (B) Wall-eyed stereo view of putative metal binding site at the external surface of EncFtnsH. Protein chains and electron density maps are shown as in (A).	FIG
+201	219	metal binding site	site	Protein chains are shown as sticks, with 2mFo-DFc electron density shown in blue mesh and contoured at 1.5 σ and mFo-DFc shown in green mesh and contoured at 3 σ. (B) Wall-eyed stereo view of putative metal binding site at the external surface of EncFtnsH. Protein chains and electron density maps are shown as in (A).	FIG
+247	255	EncFtnsH	protein	Protein chains are shown as sticks, with 2mFo-DFc electron density shown in blue mesh and contoured at 1.5 σ and mFo-DFc shown in green mesh and contoured at 3 σ. (B) Wall-eyed stereo view of putative metal binding site at the external surface of EncFtnsH. Protein chains and electron density maps are shown as in (A).	FIG
+276	297	electron density maps	evidence	Protein chains are shown as sticks, with 2mFo-DFc electron density shown in blue mesh and contoured at 1.5 σ and mFo-DFc shown in green mesh and contoured at 3 σ. (B) Wall-eyed stereo view of putative metal binding site at the external surface of EncFtnsH. Protein chains and electron density maps are shown as in (A).	FIG
+0	8	EncFtnsH	protein	EncFtnsH metal binding sites.	FIG
+9	28	metal binding sites	site	EncFtnsH metal binding sites.	FIG
+33	69	metal-binding dimerization interface	site	(A) Wall-eyed stereo view of the metal-binding dimerization interface of EncFtnsH. Protein residues are shown as sticks with blue and green carbons for the different subunits, iron ions are shown as orange spheres and calcium as grey spheres, and the glycolic acid ligand is shown with yellow carbon atoms coordinated above the di-iron center.	FIG
+73	81	EncFtnsH	protein	(A) Wall-eyed stereo view of the metal-binding dimerization interface of EncFtnsH. Protein residues are shown as sticks with blue and green carbons for the different subunits, iron ions are shown as orange spheres and calcium as grey spheres, and the glycolic acid ligand is shown with yellow carbon atoms coordinated above the di-iron center.	FIG
+166	174	subunits	structure_element	(A) Wall-eyed stereo view of the metal-binding dimerization interface of EncFtnsH. Protein residues are shown as sticks with blue and green carbons for the different subunits, iron ions are shown as orange spheres and calcium as grey spheres, and the glycolic acid ligand is shown with yellow carbon atoms coordinated above the di-iron center.	FIG
+176	180	iron	chemical	(A) Wall-eyed stereo view of the metal-binding dimerization interface of EncFtnsH. Protein residues are shown as sticks with blue and green carbons for the different subunits, iron ions are shown as orange spheres and calcium as grey spheres, and the glycolic acid ligand is shown with yellow carbon atoms coordinated above the di-iron center.	FIG
+218	225	calcium	chemical	(A) Wall-eyed stereo view of the metal-binding dimerization interface of EncFtnsH. Protein residues are shown as sticks with blue and green carbons for the different subunits, iron ions are shown as orange spheres and calcium as grey spheres, and the glycolic acid ligand is shown with yellow carbon atoms coordinated above the di-iron center.	FIG
+251	264	glycolic acid	chemical	(A) Wall-eyed stereo view of the metal-binding dimerization interface of EncFtnsH. Protein residues are shown as sticks with blue and green carbons for the different subunits, iron ions are shown as orange spheres and calcium as grey spheres, and the glycolic acid ligand is shown with yellow carbon atoms coordinated above the di-iron center.	FIG
+328	342	di-iron center	site	(A) Wall-eyed stereo view of the metal-binding dimerization interface of EncFtnsH. Protein residues are shown as sticks with blue and green carbons for the different subunits, iron ions are shown as orange spheres and calcium as grey spheres, and the glycolic acid ligand is shown with yellow carbon atoms coordinated above the di-iron center.	FIG
+4	33	2mFo-DFc electron density map	evidence	The 2mFo-DFc electron density map is shown as a blue mesh contoured at 1.5 σ and the NCS-averaged anomalous difference map is shown as an orange mesh and contoured at 10 σ. (B) Iron coordination within the FOC including residues Glu32, Glu62, His65 and Tyr39 from two chains.	FIG
+85	122	NCS-averaged anomalous difference map	evidence	The 2mFo-DFc electron density map is shown as a blue mesh contoured at 1.5 σ and the NCS-averaged anomalous difference map is shown as an orange mesh and contoured at 10 σ. (B) Iron coordination within the FOC including residues Glu32, Glu62, His65 and Tyr39 from two chains.	FIG
+177	181	Iron	chemical	The 2mFo-DFc electron density map is shown as a blue mesh contoured at 1.5 σ and the NCS-averaged anomalous difference map is shown as an orange mesh and contoured at 10 σ. (B) Iron coordination within the FOC including residues Glu32, Glu62, His65 and Tyr39 from two chains.	FIG
+182	194	coordination	bond_interaction	The 2mFo-DFc electron density map is shown as a blue mesh contoured at 1.5 σ and the NCS-averaged anomalous difference map is shown as an orange mesh and contoured at 10 σ. (B) Iron coordination within the FOC including residues Glu32, Glu62, His65 and Tyr39 from two chains.	FIG
+206	209	FOC	site	The 2mFo-DFc electron density map is shown as a blue mesh contoured at 1.5 σ and the NCS-averaged anomalous difference map is shown as an orange mesh and contoured at 10 σ. (B) Iron coordination within the FOC including residues Glu32, Glu62, His65 and Tyr39 from two chains.	FIG
+229	234	Glu32	residue_name_number	The 2mFo-DFc electron density map is shown as a blue mesh contoured at 1.5 σ and the NCS-averaged anomalous difference map is shown as an orange mesh and contoured at 10 σ. (B) Iron coordination within the FOC including residues Glu32, Glu62, His65 and Tyr39 from two chains.	FIG
+236	241	Glu62	residue_name_number	The 2mFo-DFc electron density map is shown as a blue mesh contoured at 1.5 σ and the NCS-averaged anomalous difference map is shown as an orange mesh and contoured at 10 σ. (B) Iron coordination within the FOC including residues Glu32, Glu62, His65 and Tyr39 from two chains.	FIG
+243	248	His65	residue_name_number	The 2mFo-DFc electron density map is shown as a blue mesh contoured at 1.5 σ and the NCS-averaged anomalous difference map is shown as an orange mesh and contoured at 10 σ. (B) Iron coordination within the FOC including residues Glu32, Glu62, His65 and Tyr39 from two chains.	FIG
+253	258	Tyr39	residue_name_number	The 2mFo-DFc electron density map is shown as a blue mesh contoured at 1.5 σ and the NCS-averaged anomalous difference map is shown as an orange mesh and contoured at 10 σ. (B) Iron coordination within the FOC including residues Glu32, Glu62, His65 and Tyr39 from two chains.	FIG
+42	54	Coordination	bond_interaction	Protein and metal ions are shown as in A. Coordination between the protein and iron ions is shown as yellow dashed lines with distances indicated. (C) Coordination of calcium within the dimer interface by four glutamic acid residues (E31 and E34 from two chains).	FIG
+79	83	iron	chemical	Protein and metal ions are shown as in A. Coordination between the protein and iron ions is shown as yellow dashed lines with distances indicated. (C) Coordination of calcium within the dimer interface by four glutamic acid residues (E31 and E34 from two chains).	FIG
+151	163	Coordination	bond_interaction	Protein and metal ions are shown as in A. Coordination between the protein and iron ions is shown as yellow dashed lines with distances indicated. (C) Coordination of calcium within the dimer interface by four glutamic acid residues (E31 and E34 from two chains).	FIG
+167	174	calcium	chemical	Protein and metal ions are shown as in A. Coordination between the protein and iron ions is shown as yellow dashed lines with distances indicated. (C) Coordination of calcium within the dimer interface by four glutamic acid residues (E31 and E34 from two chains).	FIG
+186	201	dimer interface	site	Protein and metal ions are shown as in A. Coordination between the protein and iron ions is shown as yellow dashed lines with distances indicated. (C) Coordination of calcium within the dimer interface by four glutamic acid residues (E31 and E34 from two chains).	FIG
+210	223	glutamic acid	residue_name	Protein and metal ions are shown as in A. Coordination between the protein and iron ions is shown as yellow dashed lines with distances indicated. (C) Coordination of calcium within the dimer interface by four glutamic acid residues (E31 and E34 from two chains).	FIG
+234	237	E31	residue_name_number	Protein and metal ions are shown as in A. Coordination between the protein and iron ions is shown as yellow dashed lines with distances indicated. (C) Coordination of calcium within the dimer interface by four glutamic acid residues (E31 and E34 from two chains).	FIG
+242	245	E34	residue_name_number	Protein and metal ions are shown as in A. Coordination between the protein and iron ions is shown as yellow dashed lines with distances indicated. (C) Coordination of calcium within the dimer interface by four glutamic acid residues (E31 and E34 from two chains).	FIG
+4	11	calcium	chemical	The calcium ion is shown as a grey sphere and water molecules involved in the coordination of the calcium ion are shown as crosses. (D) Metal coordination site on the outer surface of EncFtnsH. The two calcium ions are coordinated by residues His57, Glu61 and Glu64 from the two chains of the FOC dimer, and are located at the outer surface of the complex, positioned 10 Å away from the FOC iron.	FIG
+46	51	water	chemical	The calcium ion is shown as a grey sphere and water molecules involved in the coordination of the calcium ion are shown as crosses. (D) Metal coordination site on the outer surface of EncFtnsH. The two calcium ions are coordinated by residues His57, Glu61 and Glu64 from the two chains of the FOC dimer, and are located at the outer surface of the complex, positioned 10 Å away from the FOC iron.	FIG
+78	90	coordination	bond_interaction	The calcium ion is shown as a grey sphere and water molecules involved in the coordination of the calcium ion are shown as crosses. (D) Metal coordination site on the outer surface of EncFtnsH. The two calcium ions are coordinated by residues His57, Glu61 and Glu64 from the two chains of the FOC dimer, and are located at the outer surface of the complex, positioned 10 Å away from the FOC iron.	FIG
+98	105	calcium	chemical	The calcium ion is shown as a grey sphere and water molecules involved in the coordination of the calcium ion are shown as crosses. (D) Metal coordination site on the outer surface of EncFtnsH. The two calcium ions are coordinated by residues His57, Glu61 and Glu64 from the two chains of the FOC dimer, and are located at the outer surface of the complex, positioned 10 Å away from the FOC iron.	FIG
+136	159	Metal coordination site	site	The calcium ion is shown as a grey sphere and water molecules involved in the coordination of the calcium ion are shown as crosses. (D) Metal coordination site on the outer surface of EncFtnsH. The two calcium ions are coordinated by residues His57, Glu61 and Glu64 from the two chains of the FOC dimer, and are located at the outer surface of the complex, positioned 10 Å away from the FOC iron.	FIG
+184	192	EncFtnsH	protein	The calcium ion is shown as a grey sphere and water molecules involved in the coordination of the calcium ion are shown as crosses. (D) Metal coordination site on the outer surface of EncFtnsH. The two calcium ions are coordinated by residues His57, Glu61 and Glu64 from the two chains of the FOC dimer, and are located at the outer surface of the complex, positioned 10 Å away from the FOC iron.	FIG
+202	209	calcium	chemical	The calcium ion is shown as a grey sphere and water molecules involved in the coordination of the calcium ion are shown as crosses. (D) Metal coordination site on the outer surface of EncFtnsH. The two calcium ions are coordinated by residues His57, Glu61 and Glu64 from the two chains of the FOC dimer, and are located at the outer surface of the complex, positioned 10 Å away from the FOC iron.	FIG
+219	233	coordinated by	bond_interaction	The calcium ion is shown as a grey sphere and water molecules involved in the coordination of the calcium ion are shown as crosses. (D) Metal coordination site on the outer surface of EncFtnsH. The two calcium ions are coordinated by residues His57, Glu61 and Glu64 from the two chains of the FOC dimer, and are located at the outer surface of the complex, positioned 10 Å away from the FOC iron.	FIG
+243	248	His57	residue_name_number	The calcium ion is shown as a grey sphere and water molecules involved in the coordination of the calcium ion are shown as crosses. (D) Metal coordination site on the outer surface of EncFtnsH. The two calcium ions are coordinated by residues His57, Glu61 and Glu64 from the two chains of the FOC dimer, and are located at the outer surface of the complex, positioned 10 Å away from the FOC iron.	FIG
+250	255	Glu61	residue_name_number	The calcium ion is shown as a grey sphere and water molecules involved in the coordination of the calcium ion are shown as crosses. (D) Metal coordination site on the outer surface of EncFtnsH. The two calcium ions are coordinated by residues His57, Glu61 and Glu64 from the two chains of the FOC dimer, and are located at the outer surface of the complex, positioned 10 Å away from the FOC iron.	FIG
+260	265	Glu64	residue_name_number	The calcium ion is shown as a grey sphere and water molecules involved in the coordination of the calcium ion are shown as crosses. (D) Metal coordination site on the outer surface of EncFtnsH. The two calcium ions are coordinated by residues His57, Glu61 and Glu64 from the two chains of the FOC dimer, and are located at the outer surface of the complex, positioned 10 Å away from the FOC iron.	FIG
+293	296	FOC	site	The calcium ion is shown as a grey sphere and water molecules involved in the coordination of the calcium ion are shown as crosses. (D) Metal coordination site on the outer surface of EncFtnsH. The two calcium ions are coordinated by residues His57, Glu61 and Glu64 from the two chains of the FOC dimer, and are located at the outer surface of the complex, positioned 10 Å away from the FOC iron.	FIG
+297	302	dimer	oligomeric_state	The calcium ion is shown as a grey sphere and water molecules involved in the coordination of the calcium ion are shown as crosses. (D) Metal coordination site on the outer surface of EncFtnsH. The two calcium ions are coordinated by residues His57, Glu61 and Glu64 from the two chains of the FOC dimer, and are located at the outer surface of the complex, positioned 10 Å away from the FOC iron.	FIG
+387	390	FOC	site	The calcium ion is shown as a grey sphere and water molecules involved in the coordination of the calcium ion are shown as crosses. (D) Metal coordination site on the outer surface of EncFtnsH. The two calcium ions are coordinated by residues His57, Glu61 and Glu64 from the two chains of the FOC dimer, and are located at the outer surface of the complex, positioned 10 Å away from the FOC iron.	FIG
+391	395	iron	chemical	The calcium ion is shown as a grey sphere and water molecules involved in the coordination of the calcium ion are shown as crosses. (D) Metal coordination site on the outer surface of EncFtnsH. The two calcium ions are coordinated by residues His57, Glu61 and Glu64 from the two chains of the FOC dimer, and are located at the outer surface of the complex, positioned 10 Å away from the FOC iron.	FIG
+4	25	electron density maps	evidence	The electron density maps of the initial EncFtnsH model displayed significant positive peaks in the mFo-DFc map at the center of the 4-helix bundle dimer (Figure 5—figure supplement 1).	RESULTS
+41	49	EncFtnsH	protein	The electron density maps of the initial EncFtnsH model displayed significant positive peaks in the mFo-DFc map at the center of the 4-helix bundle dimer (Figure 5—figure supplement 1).	RESULTS
+100	111	mFo-DFc map	evidence	The electron density maps of the initial EncFtnsH model displayed significant positive peaks in the mFo-DFc map at the center of the 4-helix bundle dimer (Figure 5—figure supplement 1).	RESULTS
+133	147	4-helix bundle	structure_element	The electron density maps of the initial EncFtnsH model displayed significant positive peaks in the mFo-DFc map at the center of the 4-helix bundle dimer (Figure 5—figure supplement 1).	RESULTS
+148	153	dimer	oligomeric_state	The electron density maps of the initial EncFtnsH model displayed significant positive peaks in the mFo-DFc map at the center of the 4-helix bundle dimer (Figure 5—figure supplement 1).	RESULTS
+16	22	ICP-MS	experimental_method	Informed by the ICP-MS data indicating the presence of iron in the protein we collected diffraction data at the experimentally determined iron absorption edge (1.74 Å) and calculated an anomalous difference Fourier map using this data.	RESULTS
+43	54	presence of	protein_state	Informed by the ICP-MS data indicating the presence of iron in the protein we collected diffraction data at the experimentally determined iron absorption edge (1.74 Å) and calculated an anomalous difference Fourier map using this data.	RESULTS
+55	59	iron	chemical	Informed by the ICP-MS data indicating the presence of iron in the protein we collected diffraction data at the experimentally determined iron absorption edge (1.74 Å) and calculated an anomalous difference Fourier map using this data.	RESULTS
+88	104	diffraction data	evidence	Informed by the ICP-MS data indicating the presence of iron in the protein we collected diffraction data at the experimentally determined iron absorption edge (1.74 Å) and calculated an anomalous difference Fourier map using this data.	RESULTS
+138	142	iron	chemical	Informed by the ICP-MS data indicating the presence of iron in the protein we collected diffraction data at the experimentally determined iron absorption edge (1.74 Å) and calculated an anomalous difference Fourier map using this data.	RESULTS
+186	218	anomalous difference Fourier map	evidence	Informed by the ICP-MS data indicating the presence of iron in the protein we collected diffraction data at the experimentally determined iron absorption edge (1.74 Å) and calculated an anomalous difference Fourier map using this data.	RESULTS
+19	22	map	evidence	Inspection of this map showed two 10-sigma peaks between residues Glu32, Glu62 and His65 of two adjacent chains, and a statistically smaller 5-sigma peak between residues Glu31 and Glu34 of the two chains.	RESULTS
+43	48	peaks	evidence	Inspection of this map showed two 10-sigma peaks between residues Glu32, Glu62 and His65 of two adjacent chains, and a statistically smaller 5-sigma peak between residues Glu31 and Glu34 of the two chains.	RESULTS
+66	71	Glu32	residue_name_number	Inspection of this map showed two 10-sigma peaks between residues Glu32, Glu62 and His65 of two adjacent chains, and a statistically smaller 5-sigma peak between residues Glu31 and Glu34 of the two chains.	RESULTS
+73	78	Glu62	residue_name_number	Inspection of this map showed two 10-sigma peaks between residues Glu32, Glu62 and His65 of two adjacent chains, and a statistically smaller 5-sigma peak between residues Glu31 and Glu34 of the two chains.	RESULTS
+83	88	His65	residue_name_number	Inspection of this map showed two 10-sigma peaks between residues Glu32, Glu62 and His65 of two adjacent chains, and a statistically smaller 5-sigma peak between residues Glu31 and Glu34 of the two chains.	RESULTS
+171	176	Glu31	residue_name_number	Inspection of this map showed two 10-sigma peaks between residues Glu32, Glu62 and His65 of two adjacent chains, and a statistically smaller 5-sigma peak between residues Glu31 and Glu34 of the two chains.	RESULTS
+181	186	Glu34	residue_name_number	Inspection of this map showed two 10-sigma peaks between residues Glu32, Glu62 and His65 of two adjacent chains, and a statistically smaller 5-sigma peak between residues Glu31 and Glu34 of the two chains.	RESULTS
+41	51	refinement	experimental_method	Modeling metal ions into these peaks and refinement of the anomalous scattering parameters allowed us to identify these as two iron ions and a calcium ion respectively (Figure 5A).	RESULTS
+59	90	anomalous scattering parameters	evidence	Modeling metal ions into these peaks and refinement of the anomalous scattering parameters allowed us to identify these as two iron ions and a calcium ion respectively (Figure 5A).	RESULTS
+127	131	iron	chemical	Modeling metal ions into these peaks and refinement of the anomalous scattering parameters allowed us to identify these as two iron ions and a calcium ion respectively (Figure 5A).	RESULTS
+143	150	calcium	chemical	Modeling metal ions into these peaks and refinement of the anomalous scattering parameters allowed us to identify these as two iron ions and a calcium ion respectively (Figure 5A).	RESULTS
+35	51	electron density	evidence	An additional region of asymmetric electron density near the di-iron binding site in the mFo-DFc map was modeled as glycolic acid, presumably a breakdown product of the PEG 3350 used for crystallization.	RESULTS
+61	81	di-iron binding site	site	An additional region of asymmetric electron density near the di-iron binding site in the mFo-DFc map was modeled as glycolic acid, presumably a breakdown product of the PEG 3350 used for crystallization.	RESULTS
+89	100	mFo-DFc map	evidence	An additional region of asymmetric electron density near the di-iron binding site in the mFo-DFc map was modeled as glycolic acid, presumably a breakdown product of the PEG 3350 used for crystallization.	RESULTS
+116	129	glycolic acid	chemical	An additional region of asymmetric electron density near the di-iron binding site in the mFo-DFc map was modeled as glycolic acid, presumably a breakdown product of the PEG 3350 used for crystallization.	RESULTS
+169	177	PEG 3350	chemical	An additional region of asymmetric electron density near the di-iron binding site in the mFo-DFc map was modeled as glycolic acid, presumably a breakdown product of the PEG 3350 used for crystallization.	RESULTS
+5	19	di-iron center	site	This di-iron center has an Fe-Fe distance of 3.5 Å, Fe-Glu-O distances between 2.3 and 2.5 Å, and Fe-His-N distances of 2.5 Å (Figure 5B).	RESULTS
+27	41	Fe-Fe distance	evidence	This di-iron center has an Fe-Fe distance of 3.5 Å, Fe-Glu-O distances between 2.3 and 2.5 Å, and Fe-His-N distances of 2.5 Å (Figure 5B).	RESULTS
+52	70	Fe-Glu-O distances	evidence	This di-iron center has an Fe-Fe distance of 3.5 Å, Fe-Glu-O distances between 2.3 and 2.5 Å, and Fe-His-N distances of 2.5 Å (Figure 5B).	RESULTS
+98	116	Fe-His-N distances	evidence	This di-iron center has an Fe-Fe distance of 3.5 Å, Fe-Glu-O distances between 2.3 and 2.5 Å, and Fe-His-N distances of 2.5 Å (Figure 5B).	RESULTS
+5	17	coordination	bond_interaction	This coordination geometry is consistent with the di-nuclear ferroxidase center (FOC) found in ferritin.	RESULTS
+50	79	di-nuclear ferroxidase center	site	This coordination geometry is consistent with the di-nuclear ferroxidase center (FOC) found in ferritin.	RESULTS
+81	84	FOC	site	This coordination geometry is consistent with the di-nuclear ferroxidase center (FOC) found in ferritin.	RESULTS
+95	103	ferritin	protein_type	This coordination geometry is consistent with the di-nuclear ferroxidase center (FOC) found in ferritin.	RESULTS
+70	74	iron	chemical	It is interesting to note that although we did not add any additional iron to the crystallization trials, the FOC was fully occupied with iron in the final structure, implying that this site has a very high affinity for iron.	RESULTS
+82	104	crystallization trials	experimental_method	It is interesting to note that although we did not add any additional iron to the crystallization trials, the FOC was fully occupied with iron in the final structure, implying that this site has a very high affinity for iron.	RESULTS
+110	113	FOC	site	It is interesting to note that although we did not add any additional iron to the crystallization trials, the FOC was fully occupied with iron in the final structure, implying that this site has a very high affinity for iron.	RESULTS
+138	142	iron	chemical	It is interesting to note that although we did not add any additional iron to the crystallization trials, the FOC was fully occupied with iron in the final structure, implying that this site has a very high affinity for iron.	RESULTS
+156	165	structure	evidence	It is interesting to note that although we did not add any additional iron to the crystallization trials, the FOC was fully occupied with iron in the final structure, implying that this site has a very high affinity for iron.	RESULTS
+207	215	affinity	evidence	It is interesting to note that although we did not add any additional iron to the crystallization trials, the FOC was fully occupied with iron in the final structure, implying that this site has a very high affinity for iron.	RESULTS
+220	224	iron	chemical	It is interesting to note that although we did not add any additional iron to the crystallization trials, the FOC was fully occupied with iron in the final structure, implying that this site has a very high affinity for iron.	RESULTS
+4	11	calcium	chemical	The calcium ion coordinated by Glu31 and Glu34 adopts heptacoordinate geometry, with coordination distances of 2.5 Å between the metal ion and carboxylate oxygens of Glu31 and Glu34 (E31/34-site).	RESULTS
+16	30	coordinated by	bond_interaction	The calcium ion coordinated by Glu31 and Glu34 adopts heptacoordinate geometry, with coordination distances of 2.5 Å between the metal ion and carboxylate oxygens of Glu31 and Glu34 (E31/34-site).	RESULTS
+31	36	Glu31	residue_name_number	The calcium ion coordinated by Glu31 and Glu34 adopts heptacoordinate geometry, with coordination distances of 2.5 Å between the metal ion and carboxylate oxygens of Glu31 and Glu34 (E31/34-site).	RESULTS
+41	46	Glu34	residue_name_number	The calcium ion coordinated by Glu31 and Glu34 adopts heptacoordinate geometry, with coordination distances of 2.5 Å between the metal ion and carboxylate oxygens of Glu31 and Glu34 (E31/34-site).	RESULTS
+54	69	heptacoordinate	protein_state	The calcium ion coordinated by Glu31 and Glu34 adopts heptacoordinate geometry, with coordination distances of 2.5 Å between the metal ion and carboxylate oxygens of Glu31 and Glu34 (E31/34-site).	RESULTS
+85	97	coordination	bond_interaction	The calcium ion coordinated by Glu31 and Glu34 adopts heptacoordinate geometry, with coordination distances of 2.5 Å between the metal ion and carboxylate oxygens of Glu31 and Glu34 (E31/34-site).	RESULTS
+166	171	Glu31	residue_name_number	The calcium ion coordinated by Glu31 and Glu34 adopts heptacoordinate geometry, with coordination distances of 2.5 Å between the metal ion and carboxylate oxygens of Glu31 and Glu34 (E31/34-site).	RESULTS
+176	181	Glu34	residue_name_number	The calcium ion coordinated by Glu31 and Glu34 adopts heptacoordinate geometry, with coordination distances of 2.5 Å between the metal ion and carboxylate oxygens of Glu31 and Glu34 (E31/34-site).	RESULTS
+183	194	E31/34-site	site	The calcium ion coordinated by Glu31 and Glu34 adopts heptacoordinate geometry, with coordination distances of 2.5 Å between the metal ion and carboxylate oxygens of Glu31 and Glu34 (E31/34-site).	RESULTS
+47	58	coordinated	bond_interaction	A number of ordered solvent molecules are also coordinated to this metal ion at a distance of 2.5 Å. This heptacoordinate geometry is common in crystal structures with calcium ions (Figure 5C).	RESULTS
+106	121	heptacoordinate	protein_state	A number of ordered solvent molecules are also coordinated to this metal ion at a distance of 2.5 Å. This heptacoordinate geometry is common in crystal structures with calcium ions (Figure 5C).	RESULTS
+144	162	crystal structures	evidence	A number of ordered solvent molecules are also coordinated to this metal ion at a distance of 2.5 Å. This heptacoordinate geometry is common in crystal structures with calcium ions (Figure 5C).	RESULTS
+168	175	calcium	chemical	A number of ordered solvent molecules are also coordinated to this metal ion at a distance of 2.5 Å. This heptacoordinate geometry is common in crystal structures with calcium ions (Figure 5C).	RESULTS
+6	12	ICP-MS	experimental_method	While ICP-MS indicated that there were negligible amounts of calcium in the purified protein, the presence of 140 mM calcium acetate in the crystallization mother liquor favors the coordination of calcium at this site.	RESULTS
+61	68	calcium	chemical	While ICP-MS indicated that there were negligible amounts of calcium in the purified protein, the presence of 140 mM calcium acetate in the crystallization mother liquor favors the coordination of calcium at this site.	RESULTS
+98	109	presence of	protein_state	While ICP-MS indicated that there were negligible amounts of calcium in the purified protein, the presence of 140 mM calcium acetate in the crystallization mother liquor favors the coordination of calcium at this site.	RESULTS
+117	132	calcium acetate	chemical	While ICP-MS indicated that there were negligible amounts of calcium in the purified protein, the presence of 140 mM calcium acetate in the crystallization mother liquor favors the coordination of calcium at this site.	RESULTS
+181	193	coordination	bond_interaction	While ICP-MS indicated that there were negligible amounts of calcium in the purified protein, the presence of 140 mM calcium acetate in the crystallization mother liquor favors the coordination of calcium at this site.	RESULTS
+197	204	calcium	chemical	While ICP-MS indicated that there were negligible amounts of calcium in the purified protein, the presence of 140 mM calcium acetate in the crystallization mother liquor favors the coordination of calcium at this site.	RESULTS
+66	77	presence of	protein_state	The fact that the protein does not multimerize in solution in the presence of Fe3+ may indicate that these metal binding sites have a lower affinity for the ferric form of iron, which is the product of the ferroxidase reaction.	RESULTS
+78	82	Fe3+	chemical	The fact that the protein does not multimerize in solution in the presence of Fe3+ may indicate that these metal binding sites have a lower affinity for the ferric form of iron, which is the product of the ferroxidase reaction.	RESULTS
+107	126	metal binding sites	site	The fact that the protein does not multimerize in solution in the presence of Fe3+ may indicate that these metal binding sites have a lower affinity for the ferric form of iron, which is the product of the ferroxidase reaction.	RESULTS
+172	176	iron	chemical	The fact that the protein does not multimerize in solution in the presence of Fe3+ may indicate that these metal binding sites have a lower affinity for the ferric form of iron, which is the product of the ferroxidase reaction.	RESULTS
+206	217	ferroxidase	protein_type	The fact that the protein does not multimerize in solution in the presence of Fe3+ may indicate that these metal binding sites have a lower affinity for the ferric form of iron, which is the product of the ferroxidase reaction.	RESULTS
+90	97	decamer	oligomeric_state	A number of additional metal-ions were present at the outer circumference of at least one decamer in the asymmetric unit (Figure 5D).	RESULTS
+15	29	coordinated by	bond_interaction	These ions are coordinated by His57, Glu61 and Glu64 from both chains in the FOC dimer and are 4.5 Å apart; Fe-Glu-O distances are between 2.5 and 3.5 Å and the Fe-His-N distances are 4 and 4.5 Å.	RESULTS
+30	35	His57	residue_name_number	These ions are coordinated by His57, Glu61 and Glu64 from both chains in the FOC dimer and are 4.5 Å apart; Fe-Glu-O distances are between 2.5 and 3.5 Å and the Fe-His-N distances are 4 and 4.5 Å.	RESULTS
+37	42	Glu61	residue_name_number	These ions are coordinated by His57, Glu61 and Glu64 from both chains in the FOC dimer and are 4.5 Å apart; Fe-Glu-O distances are between 2.5 and 3.5 Å and the Fe-His-N distances are 4 and 4.5 Å.	RESULTS
+47	52	Glu64	residue_name_number	These ions are coordinated by His57, Glu61 and Glu64 from both chains in the FOC dimer and are 4.5 Å apart; Fe-Glu-O distances are between 2.5 and 3.5 Å and the Fe-His-N distances are 4 and 4.5 Å.	RESULTS
+77	80	FOC	site	These ions are coordinated by His57, Glu61 and Glu64 from both chains in the FOC dimer and are 4.5 Å apart; Fe-Glu-O distances are between 2.5 and 3.5 Å and the Fe-His-N distances are 4 and 4.5 Å.	RESULTS
+81	86	dimer	oligomeric_state	These ions are coordinated by His57, Glu61 and Glu64 from both chains in the FOC dimer and are 4.5 Å apart; Fe-Glu-O distances are between 2.5 and 3.5 Å and the Fe-His-N distances are 4 and 4.5 Å.	RESULTS
+108	116	Fe-Glu-O	evidence	These ions are coordinated by His57, Glu61 and Glu64 from both chains in the FOC dimer and are 4.5 Å apart; Fe-Glu-O distances are between 2.5 and 3.5 Å and the Fe-His-N distances are 4 and 4.5 Å.	RESULTS
+161	179	Fe-His-N distances	evidence	These ions are coordinated by His57, Glu61 and Glu64 from both chains in the FOC dimer and are 4.5 Å apart; Fe-Glu-O distances are between 2.5 and 3.5 Å and the Fe-His-N distances are 4 and 4.5 Å.	RESULTS
+38	46	EncFtnsH	protein	Comparison of quaternary structure of EncFtnsH and ferritin.	FIG
+51	59	ferritin	protein_type	Comparison of quaternary structure of EncFtnsH and ferritin.	FIG
+4	11	Aligned	experimental_method	(A) Aligned FOC of EncFtnsH and Pseudo-nitzschia multiseries ferritin (PmFtn).	FIG
+12	15	FOC	site	(A) Aligned FOC of EncFtnsH and Pseudo-nitzschia multiseries ferritin (PmFtn).	FIG
+19	27	EncFtnsH	protein	(A) Aligned FOC of EncFtnsH and Pseudo-nitzschia multiseries ferritin (PmFtn).	FIG
+32	60	Pseudo-nitzschia multiseries	species	(A) Aligned FOC of EncFtnsH and Pseudo-nitzschia multiseries ferritin (PmFtn).	FIG
+61	69	ferritin	protein	(A) Aligned FOC of EncFtnsH and Pseudo-nitzschia multiseries ferritin (PmFtn).	FIG
+71	76	PmFtn	protein	(A) Aligned FOC of EncFtnsH and Pseudo-nitzschia multiseries ferritin (PmFtn).	FIG
+4	22	metal binding site	site	The metal binding site residues from two EncFtnsH chains are shown in green and blue, while the PmFtn is shown in orange.	FIG
+41	49	EncFtnsH	protein	The metal binding site residues from two EncFtnsH chains are shown in green and blue, while the PmFtn is shown in orange.	FIG
+96	101	PmFtn	protein	The metal binding site residues from two EncFtnsH chains are shown in green and blue, while the PmFtn is shown in orange.	FIG
+0	4	Fe2+	chemical	Fe2+ in the FOC is shown as orange spheres and Ca2+ in EncFtnsH is shown as a grey sphere.	FIG
+12	15	FOC	site	Fe2+ in the FOC is shown as orange spheres and Ca2+ in EncFtnsH is shown as a grey sphere.	FIG
+47	51	Ca2+	chemical	Fe2+ in the FOC is shown as orange spheres and Ca2+ in EncFtnsH is shown as a grey sphere.	FIG
+55	63	EncFtnsH	protein	Fe2+ in the FOC is shown as orange spheres and Ca2+ in EncFtnsH is shown as a grey sphere.	FIG
+34	40	EncFtn	protein	The two-fold symmetry axis of the EncFtn FOC is shown with a grey arrow (B) Cross-section surface view of quaternary structure of EncFtnsH and PmFtn as aligned in (A) (dashed black box).	FIG
+41	44	FOC	site	The two-fold symmetry axis of the EncFtn FOC is shown with a grey arrow (B) Cross-section surface view of quaternary structure of EncFtnsH and PmFtn as aligned in (A) (dashed black box).	FIG
+130	138	EncFtnsH	protein	The two-fold symmetry axis of the EncFtn FOC is shown with a grey arrow (B) Cross-section surface view of quaternary structure of EncFtnsH and PmFtn as aligned in (A) (dashed black box).	FIG
+143	148	PmFtn	protein	The two-fold symmetry axis of the EncFtn FOC is shown with a grey arrow (B) Cross-section surface view of quaternary structure of EncFtnsH and PmFtn as aligned in (A) (dashed black box).	FIG
+4	19	central channel	site	The central channel of EncFtnsH is spatially equivalent to the outer surface of ferritin and its outer surface corresponds to the mineralization surface within ferritin.	FIG
+23	31	EncFtnsH	protein	The central channel of EncFtnsH is spatially equivalent to the outer surface of ferritin and its outer surface corresponds to the mineralization surface within ferritin.	FIG
+80	88	ferritin	protein_type	The central channel of EncFtnsH is spatially equivalent to the outer surface of ferritin and its outer surface corresponds to the mineralization surface within ferritin.	FIG
+130	152	mineralization surface	site	The central channel of EncFtnsH is spatially equivalent to the outer surface of ferritin and its outer surface corresponds to the mineralization surface within ferritin.	FIG
+160	168	ferritin	protein_type	The central channel of EncFtnsH is spatially equivalent to the outer surface of ferritin and its outer surface corresponds to the mineralization surface within ferritin.	FIG
+0	10	Comparison	experimental_method	Comparison of the symmetric metal ion binding site of EncFtnsH and the ferritin FOC.	FIG
+28	50	metal ion binding site	site	Comparison of the symmetric metal ion binding site of EncFtnsH and the ferritin FOC.	FIG
+54	62	EncFtnsH	protein	Comparison of the symmetric metal ion binding site of EncFtnsH and the ferritin FOC.	FIG
+71	79	ferritin	protein_type	Comparison of the symmetric metal ion binding site of EncFtnsH and the ferritin FOC.	FIG
+80	83	FOC	site	Comparison of the symmetric metal ion binding site of EncFtnsH and the ferritin FOC.	FIG
+4	24	Structural alignment	experimental_method	(A) Structural alignment of the FOC residues in a dimer of EncFtnsH (green/blue) with a monomer of Pseudo-nitzschia multiseries ferritin (PmFtn) (PDBID: 4ITW) (orange).	FIG
+32	35	FOC	site	(A) Structural alignment of the FOC residues in a dimer of EncFtnsH (green/blue) with a monomer of Pseudo-nitzschia multiseries ferritin (PmFtn) (PDBID: 4ITW) (orange).	FIG
+50	55	dimer	oligomeric_state	(A) Structural alignment of the FOC residues in a dimer of EncFtnsH (green/blue) with a monomer of Pseudo-nitzschia multiseries ferritin (PmFtn) (PDBID: 4ITW) (orange).	FIG
+59	67	EncFtnsH	protein	(A) Structural alignment of the FOC residues in a dimer of EncFtnsH (green/blue) with a monomer of Pseudo-nitzschia multiseries ferritin (PmFtn) (PDBID: 4ITW) (orange).	FIG
+88	95	monomer	oligomeric_state	(A) Structural alignment of the FOC residues in a dimer of EncFtnsH (green/blue) with a monomer of Pseudo-nitzschia multiseries ferritin (PmFtn) (PDBID: 4ITW) (orange).	FIG
+99	127	Pseudo-nitzschia multiseries	species	(A) Structural alignment of the FOC residues in a dimer of EncFtnsH (green/blue) with a monomer of Pseudo-nitzschia multiseries ferritin (PmFtn) (PDBID: 4ITW) (orange).	FIG
+128	136	ferritin	protein	(A) Structural alignment of the FOC residues in a dimer of EncFtnsH (green/blue) with a monomer of Pseudo-nitzschia multiseries ferritin (PmFtn) (PDBID: 4ITW) (orange).	FIG
+138	143	PmFtn	protein	(A) Structural alignment of the FOC residues in a dimer of EncFtnsH (green/blue) with a monomer of Pseudo-nitzschia multiseries ferritin (PmFtn) (PDBID: 4ITW) (orange).	FIG
+0	4	Iron	chemical	Iron ions are shown as orange spheres and a single calcium ion as a grey sphere.	FIG
+51	58	calcium	chemical	Iron ions are shown as orange spheres and a single calcium ion as a grey sphere.	FIG
+20	23	FOC	site	Residues within the FOC are conserved between EncFtn and ferritin PmFtn, with the exception of residues in the position equivalent to H65’ in the second subunit in the dimer (blue).	FIG
+28	37	conserved	protein_state	Residues within the FOC are conserved between EncFtn and ferritin PmFtn, with the exception of residues in the position equivalent to H65’ in the second subunit in the dimer (blue).	FIG
+46	52	EncFtn	protein	Residues within the FOC are conserved between EncFtn and ferritin PmFtn, with the exception of residues in the position equivalent to H65’ in the second subunit in the dimer (blue).	FIG
+57	65	ferritin	protein_type	Residues within the FOC are conserved between EncFtn and ferritin PmFtn, with the exception of residues in the position equivalent to H65’ in the second subunit in the dimer (blue).	FIG
+66	71	PmFtn	protein	Residues within the FOC are conserved between EncFtn and ferritin PmFtn, with the exception of residues in the position equivalent to H65’ in the second subunit in the dimer (blue).	FIG
+134	137	H65	residue_name_number	Residues within the FOC are conserved between EncFtn and ferritin PmFtn, with the exception of residues in the position equivalent to H65’ in the second subunit in the dimer (blue).	FIG
+153	160	subunit	oligomeric_state	Residues within the FOC are conserved between EncFtn and ferritin PmFtn, with the exception of residues in the position equivalent to H65’ in the second subunit in the dimer (blue).	FIG
+168	173	dimer	oligomeric_state	Residues within the FOC are conserved between EncFtn and ferritin PmFtn, with the exception of residues in the position equivalent to H65’ in the second subunit in the dimer (blue).	FIG
+12	18	EncFtn	protein	The site in EncFtn with bound calcium is not present in other family members.	FIG
+24	29	bound	protein_state	The site in EncFtn with bound calcium is not present in other family members.	FIG
+30	37	calcium	chemical	The site in EncFtn with bound calcium is not present in other family members.	FIG
+27	34	aligned	experimental_method	(B) Secondary structure of aligned dimeric EncFtnsH and monomeric ferritin highlighting the conserved four-helix bundle.	FIG
+35	42	dimeric	oligomeric_state	(B) Secondary structure of aligned dimeric EncFtnsH and monomeric ferritin highlighting the conserved four-helix bundle.	FIG
+43	51	EncFtnsH	protein	(B) Secondary structure of aligned dimeric EncFtnsH and monomeric ferritin highlighting the conserved four-helix bundle.	FIG
+56	65	monomeric	oligomeric_state	(B) Secondary structure of aligned dimeric EncFtnsH and monomeric ferritin highlighting the conserved four-helix bundle.	FIG
+66	74	ferritin	protein_type	(B) Secondary structure of aligned dimeric EncFtnsH and monomeric ferritin highlighting the conserved four-helix bundle.	FIG
+92	101	conserved	protein_state	(B) Secondary structure of aligned dimeric EncFtnsH and monomeric ferritin highlighting the conserved four-helix bundle.	FIG
+102	119	four-helix bundle	structure_element	(B) Secondary structure of aligned dimeric EncFtnsH and monomeric ferritin highlighting the conserved four-helix bundle.	FIG
+0	8	EncFtnsH	protein	EncFtnsH monomers are shown in green and blue and aligned PmFtn monomer in orange as in A. (C) Cartoon of secondary structure elements in EncFtn dimer and ferritin.	FIG
+9	17	monomers	oligomeric_state	EncFtnsH monomers are shown in green and blue and aligned PmFtn monomer in orange as in A. (C) Cartoon of secondary structure elements in EncFtn dimer and ferritin.	FIG
+50	57	aligned	experimental_method	EncFtnsH monomers are shown in green and blue and aligned PmFtn monomer in orange as in A. (C) Cartoon of secondary structure elements in EncFtn dimer and ferritin.	FIG
+58	63	PmFtn	protein	EncFtnsH monomers are shown in green and blue and aligned PmFtn monomer in orange as in A. (C) Cartoon of secondary structure elements in EncFtn dimer and ferritin.	FIG
+64	71	monomer	oligomeric_state	EncFtnsH monomers are shown in green and blue and aligned PmFtn monomer in orange as in A. (C) Cartoon of secondary structure elements in EncFtn dimer and ferritin.	FIG
+138	144	EncFtn	protein	EncFtnsH monomers are shown in green and blue and aligned PmFtn monomer in orange as in A. (C) Cartoon of secondary structure elements in EncFtn dimer and ferritin.	FIG
+145	150	dimer	oligomeric_state	EncFtnsH monomers are shown in green and blue and aligned PmFtn monomer in orange as in A. (C) Cartoon of secondary structure elements in EncFtn dimer and ferritin.	FIG
+155	163	ferritin	protein_type	EncFtnsH monomers are shown in green and blue and aligned PmFtn monomer in orange as in A. (C) Cartoon of secondary structure elements in EncFtn dimer and ferritin.	FIG
+7	12	dimer	oligomeric_state	In the dimer of EncFtn that forms the FOC, the C-terminus of the first monomer (green) and N-terminus of the second monomer (blue) correspond to the position of the long linker between α2 and α3 in ferritin PmFtn.	FIG
+16	22	EncFtn	protein	In the dimer of EncFtn that forms the FOC, the C-terminus of the first monomer (green) and N-terminus of the second monomer (blue) correspond to the position of the long linker between α2 and α3 in ferritin PmFtn.	FIG
+38	41	FOC	site	In the dimer of EncFtn that forms the FOC, the C-terminus of the first monomer (green) and N-terminus of the second monomer (blue) correspond to the position of the long linker between α2 and α3 in ferritin PmFtn.	FIG
+71	78	monomer	oligomeric_state	In the dimer of EncFtn that forms the FOC, the C-terminus of the first monomer (green) and N-terminus of the second monomer (blue) correspond to the position of the long linker between α2 and α3 in ferritin PmFtn.	FIG
+116	123	monomer	oligomeric_state	In the dimer of EncFtn that forms the FOC, the C-terminus of the first monomer (green) and N-terminus of the second monomer (blue) correspond to the position of the long linker between α2 and α3 in ferritin PmFtn.	FIG
+165	176	long linker	structure_element	In the dimer of EncFtn that forms the FOC, the C-terminus of the first monomer (green) and N-terminus of the second monomer (blue) correspond to the position of the long linker between α2 and α3 in ferritin PmFtn.	FIG
+185	187	α2	structure_element	In the dimer of EncFtn that forms the FOC, the C-terminus of the first monomer (green) and N-terminus of the second monomer (blue) correspond to the position of the long linker between α2 and α3 in ferritin PmFtn.	FIG
+192	194	α3	structure_element	In the dimer of EncFtn that forms the FOC, the C-terminus of the first monomer (green) and N-terminus of the second monomer (blue) correspond to the position of the long linker between α2 and α3 in ferritin PmFtn.	FIG
+198	206	ferritin	protein_type	In the dimer of EncFtn that forms the FOC, the C-terminus of the first monomer (green) and N-terminus of the second monomer (blue) correspond to the position of the long linker between α2 and α3 in ferritin PmFtn.	FIG
+207	212	PmFtn	protein	In the dimer of EncFtn that forms the FOC, the C-terminus of the first monomer (green) and N-terminus of the second monomer (blue) correspond to the position of the long linker between α2 and α3 in ferritin PmFtn.	FIG
+0	20	Structural alignment	experimental_method	Structural alignment of the di-iron binding site of EncFtnsH to the FOC of Pseudo-nitzschia multiseries ferritin (PmFtn, PDB ID: 4ITW) reveals a striking similarity between the metal binding sites of EncFtnsH and the classical ferritins  (Figure 6A).	RESULTS
+28	48	di-iron binding site	site	Structural alignment of the di-iron binding site of EncFtnsH to the FOC of Pseudo-nitzschia multiseries ferritin (PmFtn, PDB ID: 4ITW) reveals a striking similarity between the metal binding sites of EncFtnsH and the classical ferritins  (Figure 6A).	RESULTS
+52	60	EncFtnsH	protein	Structural alignment of the di-iron binding site of EncFtnsH to the FOC of Pseudo-nitzschia multiseries ferritin (PmFtn, PDB ID: 4ITW) reveals a striking similarity between the metal binding sites of EncFtnsH and the classical ferritins  (Figure 6A).	RESULTS
+68	71	FOC	site	Structural alignment of the di-iron binding site of EncFtnsH to the FOC of Pseudo-nitzschia multiseries ferritin (PmFtn, PDB ID: 4ITW) reveals a striking similarity between the metal binding sites of EncFtnsH and the classical ferritins  (Figure 6A).	RESULTS
+75	103	Pseudo-nitzschia multiseries	species	Structural alignment of the di-iron binding site of EncFtnsH to the FOC of Pseudo-nitzschia multiseries ferritin (PmFtn, PDB ID: 4ITW) reveals a striking similarity between the metal binding sites of EncFtnsH and the classical ferritins  (Figure 6A).	RESULTS
+104	112	ferritin	protein_type	Structural alignment of the di-iron binding site of EncFtnsH to the FOC of Pseudo-nitzschia multiseries ferritin (PmFtn, PDB ID: 4ITW) reveals a striking similarity between the metal binding sites of EncFtnsH and the classical ferritins  (Figure 6A).	RESULTS
+114	119	PmFtn	protein	Structural alignment of the di-iron binding site of EncFtnsH to the FOC of Pseudo-nitzschia multiseries ferritin (PmFtn, PDB ID: 4ITW) reveals a striking similarity between the metal binding sites of EncFtnsH and the classical ferritins  (Figure 6A).	RESULTS
+177	196	metal binding sites	site	Structural alignment of the di-iron binding site of EncFtnsH to the FOC of Pseudo-nitzschia multiseries ferritin (PmFtn, PDB ID: 4ITW) reveals a striking similarity between the metal binding sites of EncFtnsH and the classical ferritins  (Figure 6A).	RESULTS
+200	208	EncFtnsH	protein	Structural alignment of the di-iron binding site of EncFtnsH to the FOC of Pseudo-nitzschia multiseries ferritin (PmFtn, PDB ID: 4ITW) reveals a striking similarity between the metal binding sites of EncFtnsH and the classical ferritins  (Figure 6A).	RESULTS
+217	226	classical	protein_state	Structural alignment of the di-iron binding site of EncFtnsH to the FOC of Pseudo-nitzschia multiseries ferritin (PmFtn, PDB ID: 4ITW) reveals a striking similarity between the metal binding sites of EncFtnsH and the classical ferritins  (Figure 6A).	RESULTS
+227	236	ferritins	protein_type	Structural alignment of the di-iron binding site of EncFtnsH to the FOC of Pseudo-nitzschia multiseries ferritin (PmFtn, PDB ID: 4ITW) reveals a striking similarity between the metal binding sites of EncFtnsH and the classical ferritins  (Figure 6A).	RESULTS
+4	16	di-iron site	site	The di-iron site of EncFtnsH is by necessity symmetrical, as it is formed through a dimer interface, while the FOC of ferritin does not have these constraints and varies in different species at a position equivalent to His65 of the second EncFtn monomer in the FOC interface (His65’) (Figure 6A).	RESULTS
+20	28	EncFtnsH	protein	The di-iron site of EncFtnsH is by necessity symmetrical, as it is formed through a dimer interface, while the FOC of ferritin does not have these constraints and varies in different species at a position equivalent to His65 of the second EncFtn monomer in the FOC interface (His65’) (Figure 6A).	RESULTS
+84	99	dimer interface	site	The di-iron site of EncFtnsH is by necessity symmetrical, as it is formed through a dimer interface, while the FOC of ferritin does not have these constraints and varies in different species at a position equivalent to His65 of the second EncFtn monomer in the FOC interface (His65’) (Figure 6A).	RESULTS
+111	114	FOC	site	The di-iron site of EncFtnsH is by necessity symmetrical, as it is formed through a dimer interface, while the FOC of ferritin does not have these constraints and varies in different species at a position equivalent to His65 of the second EncFtn monomer in the FOC interface (His65’) (Figure 6A).	RESULTS
+118	126	ferritin	protein_type	The di-iron site of EncFtnsH is by necessity symmetrical, as it is formed through a dimer interface, while the FOC of ferritin does not have these constraints and varies in different species at a position equivalent to His65 of the second EncFtn monomer in the FOC interface (His65’) (Figure 6A).	RESULTS
+219	224	His65	residue_name_number	The di-iron site of EncFtnsH is by necessity symmetrical, as it is formed through a dimer interface, while the FOC of ferritin does not have these constraints and varies in different species at a position equivalent to His65 of the second EncFtn monomer in the FOC interface (His65’) (Figure 6A).	RESULTS
+239	245	EncFtn	protein	The di-iron site of EncFtnsH is by necessity symmetrical, as it is formed through a dimer interface, while the FOC of ferritin does not have these constraints and varies in different species at a position equivalent to His65 of the second EncFtn monomer in the FOC interface (His65’) (Figure 6A).	RESULTS
+246	253	monomer	oligomeric_state	The di-iron site of EncFtnsH is by necessity symmetrical, as it is formed through a dimer interface, while the FOC of ferritin does not have these constraints and varies in different species at a position equivalent to His65 of the second EncFtn monomer in the FOC interface (His65’) (Figure 6A).	RESULTS
+261	274	FOC interface	site	The di-iron site of EncFtnsH is by necessity symmetrical, as it is formed through a dimer interface, while the FOC of ferritin does not have these constraints and varies in different species at a position equivalent to His65 of the second EncFtn monomer in the FOC interface (His65’) (Figure 6A).	RESULTS
+276	281	His65	residue_name_number	The di-iron site of EncFtnsH is by necessity symmetrical, as it is formed through a dimer interface, while the FOC of ferritin does not have these constraints and varies in different species at a position equivalent to His65 of the second EncFtn monomer in the FOC interface (His65’) (Figure 6A).	RESULTS
+0	26	Structural superimposition	experimental_method	Structural superimposition of the FOCs of ferritin and EncFtn brings the four-helix bundle of the ferritin fold into close alignment with the EncFtn dimer, showing that the two families of proteins have essentially the same architecture around the di-iron center (Figure 6B).	RESULTS
+34	38	FOCs	site	Structural superimposition of the FOCs of ferritin and EncFtn brings the four-helix bundle of the ferritin fold into close alignment with the EncFtn dimer, showing that the two families of proteins have essentially the same architecture around the di-iron center (Figure 6B).	RESULTS
+42	50	ferritin	protein_type	Structural superimposition of the FOCs of ferritin and EncFtn brings the four-helix bundle of the ferritin fold into close alignment with the EncFtn dimer, showing that the two families of proteins have essentially the same architecture around the di-iron center (Figure 6B).	RESULTS
+55	61	EncFtn	protein	Structural superimposition of the FOCs of ferritin and EncFtn brings the four-helix bundle of the ferritin fold into close alignment with the EncFtn dimer, showing that the two families of proteins have essentially the same architecture around the di-iron center (Figure 6B).	RESULTS
+73	90	four-helix bundle	structure_element	Structural superimposition of the FOCs of ferritin and EncFtn brings the four-helix bundle of the ferritin fold into close alignment with the EncFtn dimer, showing that the two families of proteins have essentially the same architecture around the di-iron center (Figure 6B).	RESULTS
+98	106	ferritin	protein_type	Structural superimposition of the FOCs of ferritin and EncFtn brings the four-helix bundle of the ferritin fold into close alignment with the EncFtn dimer, showing that the two families of proteins have essentially the same architecture around the di-iron center (Figure 6B).	RESULTS
+142	148	EncFtn	protein	Structural superimposition of the FOCs of ferritin and EncFtn brings the four-helix bundle of the ferritin fold into close alignment with the EncFtn dimer, showing that the two families of proteins have essentially the same architecture around the di-iron center (Figure 6B).	RESULTS
+149	154	dimer	oligomeric_state	Structural superimposition of the FOCs of ferritin and EncFtn brings the four-helix bundle of the ferritin fold into close alignment with the EncFtn dimer, showing that the two families of proteins have essentially the same architecture around the di-iron center (Figure 6B).	RESULTS
+248	262	di-iron center	site	Structural superimposition of the FOCs of ferritin and EncFtn brings the four-helix bundle of the ferritin fold into close alignment with the EncFtn dimer, showing that the two families of proteins have essentially the same architecture around the di-iron center (Figure 6B).	RESULTS
+4	10	linker	structure_element	The linker connecting helices 2 and 3 of ferritin is congruent with the start of the C-terminal helix of one EncFtn monomer and the N-terminal 310 helix of the second monomer (Figure 6C).	RESULTS
+22	37	helices 2 and 3	structure_element	The linker connecting helices 2 and 3 of ferritin is congruent with the start of the C-terminal helix of one EncFtn monomer and the N-terminal 310 helix of the second monomer (Figure 6C).	RESULTS
+41	49	ferritin	protein_type	The linker connecting helices 2 and 3 of ferritin is congruent with the start of the C-terminal helix of one EncFtn monomer and the N-terminal 310 helix of the second monomer (Figure 6C).	RESULTS
+96	101	helix	structure_element	The linker connecting helices 2 and 3 of ferritin is congruent with the start of the C-terminal helix of one EncFtn monomer and the N-terminal 310 helix of the second monomer (Figure 6C).	RESULTS
+109	115	EncFtn	protein	The linker connecting helices 2 and 3 of ferritin is congruent with the start of the C-terminal helix of one EncFtn monomer and the N-terminal 310 helix of the second monomer (Figure 6C).	RESULTS
+116	123	monomer	oligomeric_state	The linker connecting helices 2 and 3 of ferritin is congruent with the start of the C-terminal helix of one EncFtn monomer and the N-terminal 310 helix of the second monomer (Figure 6C).	RESULTS
+143	152	310 helix	structure_element	The linker connecting helices 2 and 3 of ferritin is congruent with the start of the C-terminal helix of one EncFtn monomer and the N-terminal 310 helix of the second monomer (Figure 6C).	RESULTS
+167	174	monomer	oligomeric_state	The linker connecting helices 2 and 3 of ferritin is congruent with the start of the C-terminal helix of one EncFtn monomer and the N-terminal 310 helix of the second monomer (Figure 6C).	RESULTS
+0	17	Mass spectrometry	experimental_method	Mass spectrometry of the EncFtn assembly	RESULTS
+25	31	EncFtn	protein	Mass spectrometry of the EncFtn assembly	RESULTS
+0	12	Native IM-MS	experimental_method	Native IM-MS analysis of the apo-EncFtnsH monomer.	FIG
+29	32	apo	protein_state	Native IM-MS analysis of the apo-EncFtnsH monomer.	FIG
+33	41	EncFtnsH	protein	Native IM-MS analysis of the apo-EncFtnsH monomer.	FIG
+42	49	monomer	oligomeric_state	Native IM-MS analysis of the apo-EncFtnsH monomer.	FIG
+4	17	Mass spectrum	evidence	(A) Mass spectrum of apo-EncFtnsH acquired from 100 mM ammonium acetate pH 8.0 under native MS conditions.	FIG
+21	24	apo	protein_state	(A) Mass spectrum of apo-EncFtnsH acquired from 100 mM ammonium acetate pH 8.0 under native MS conditions.	FIG
+25	33	EncFtnsH	protein	(A) Mass spectrum of apo-EncFtnsH acquired from 100 mM ammonium acetate pH 8.0 under native MS conditions.	FIG
+85	94	native MS	experimental_method	(A) Mass spectrum of apo-EncFtnsH acquired from 100 mM ammonium acetate pH 8.0 under native MS conditions.	FIG
+4	16	charge state	evidence	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+56	61	peaks	evidence	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+93	106	charge states	evidence	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+110	113	apo	protein_state	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+114	121	monomer	oligomeric_state	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+122	130	EncFtnsH	protein	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+175	201	arrival time distributions	evidence	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+203	220	ion mobility data	evidence	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+241	244	apo	protein_state	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+245	253	EncFtnsH	protein	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+254	266	charge state	evidence	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+355	380	arrival time distribution	evidence	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+415	427	charge state	evidence	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+485	511	arrival time distributions	evidence	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+567	590	collision cross section	evidence	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+592	593	Ω	evidence	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+609	632	collision cross section	evidence	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+645	652	monomer	oligomeric_state	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+667	684	crystal structure	evidence	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+692	701	Fe-loaded	protein_state	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+702	710	EncFtnsH	protein	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+711	718	decamer	oligomeric_state	The charge state distribution observed is bimodal, with peaks corresponding to the 6+ to 15+ charge states of apo-monomer EncFtnsH (neutral average mass 13,194.3 Da). (B) The arrival time distributions (ion mobility data) of all ions in the apo-EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale). (B) Right, the arrival time distribution of the 6+ (orange) and 7+ (green) charge state (dashed colored‐box) has been extracted and plotted; The arrival time distributions for these ion is shown (ms), along with the calibrated collision cross section, Ω (nm2). (C) The collision cross section of a single monomer unit from the crystal structure of the Fe-loaded EncFtnsH decamer was calculated to be 15.8 nm2 using IMPACT v. 0.9.1.	FIG
+22	35	charge states	evidence	The +8 to +15 protein charge states have observed CCS between 20–26 nm2, which is significantly higher than the calculated CCS for an EncFtnsH monomer taken from the decameric assembly crystal structure (15.8 nm2).	FIG
+50	53	CCS	evidence	The +8 to +15 protein charge states have observed CCS between 20–26 nm2, which is significantly higher than the calculated CCS for an EncFtnsH monomer taken from the decameric assembly crystal structure (15.8 nm2).	FIG
+123	126	CCS	evidence	The +8 to +15 protein charge states have observed CCS between 20–26 nm2, which is significantly higher than the calculated CCS for an EncFtnsH monomer taken from the decameric assembly crystal structure (15.8 nm2).	FIG
+134	142	EncFtnsH	protein	The +8 to +15 protein charge states have observed CCS between 20–26 nm2, which is significantly higher than the calculated CCS for an EncFtnsH monomer taken from the decameric assembly crystal structure (15.8 nm2).	FIG
+143	150	monomer	oligomeric_state	The +8 to +15 protein charge states have observed CCS between 20–26 nm2, which is significantly higher than the calculated CCS for an EncFtnsH monomer taken from the decameric assembly crystal structure (15.8 nm2).	FIG
+166	175	decameric	oligomeric_state	The +8 to +15 protein charge states have observed CCS between 20–26 nm2, which is significantly higher than the calculated CCS for an EncFtnsH monomer taken from the decameric assembly crystal structure (15.8 nm2).	FIG
+185	202	crystal structure	evidence	The +8 to +15 protein charge states have observed CCS between 20–26 nm2, which is significantly higher than the calculated CCS for an EncFtnsH monomer taken from the decameric assembly crystal structure (15.8 nm2).	FIG
+4	12	mobility	evidence	The mobility of the +7 charge state displays broad drift-time distribution with maxima consistent with CCS of 15.9 and 17.9 nm2.	FIG
+23	35	charge state	evidence	The mobility of the +7 charge state displays broad drift-time distribution with maxima consistent with CCS of 15.9 and 17.9 nm2.	FIG
+51	74	drift-time distribution	evidence	The mobility of the +7 charge state displays broad drift-time distribution with maxima consistent with CCS of 15.9 and 17.9 nm2.	FIG
+103	106	CCS	evidence	The mobility of the +7 charge state displays broad drift-time distribution with maxima consistent with CCS of 15.9 and 17.9 nm2.	FIG
+16	28	charge state	evidence	Finally, the 6+ charge state of EncFtnsH has mobility consistent with a CCS of 12.3 nm2, indicating a more compact/collapsed structure.	FIG
+32	40	EncFtnsH	protein	Finally, the 6+ charge state of EncFtnsH has mobility consistent with a CCS of 12.3 nm2, indicating a more compact/collapsed structure.	FIG
+45	53	mobility	evidence	Finally, the 6+ charge state of EncFtnsH has mobility consistent with a CCS of 12.3 nm2, indicating a more compact/collapsed structure.	FIG
+72	75	CCS	evidence	Finally, the 6+ charge state of EncFtnsH has mobility consistent with a CCS of 12.3 nm2, indicating a more compact/collapsed structure.	FIG
+107	114	compact	protein_state	Finally, the 6+ charge state of EncFtnsH has mobility consistent with a CCS of 12.3 nm2, indicating a more compact/collapsed structure.	FIG
+115	124	collapsed	protein_state	Finally, the 6+ charge state of EncFtnsH has mobility consistent with a CCS of 12.3 nm2, indicating a more compact/collapsed structure.	FIG
+32	35	apo	protein_state	It is clear from this data that apo-EncFtnsH exists in several gas phase conformations.	FIG
+36	44	EncFtnsH	protein	It is clear from this data that apo-EncFtnsH exists in several gas phase conformations.	FIG
+13	26	charge states	evidence	The range of charge states occupied by the protein (6+ to 15+) and the range of CCS in which the protein is observed (12.3 nm2 – 26 nm2) are both large.	FIG
+80	83	CCS	evidence	The range of charge states occupied by the protein (6+ to 15+) and the range of CCS in which the protein is observed (12.3 nm2 – 26 nm2) are both large.	FIG
+25	38	charge states	evidence	In addition, many of the charge states observed have higher charge than the theoretical maximal charge on spherical globular protein, as determined by the De La Mora relationship (ZR = 0.0778m; for the EncFtnsH monomer ZR = 8.9) Fernandez.	FIG
+116	124	globular	protein_state	In addition, many of the charge states observed have higher charge than the theoretical maximal charge on spherical globular protein, as determined by the De La Mora relationship (ZR = 0.0778m; for the EncFtnsH monomer ZR = 8.9) Fernandez.	FIG
+155	178	De La Mora relationship	experimental_method	In addition, many of the charge states observed have higher charge than the theoretical maximal charge on spherical globular protein, as determined by the De La Mora relationship (ZR = 0.0778m; for the EncFtnsH monomer ZR = 8.9) Fernandez.	FIG
+180	182	ZR	evidence	In addition, many of the charge states observed have higher charge than the theoretical maximal charge on spherical globular protein, as determined by the De La Mora relationship (ZR = 0.0778m; for the EncFtnsH monomer ZR = 8.9) Fernandez.	FIG
+202	210	EncFtnsH	protein	In addition, many of the charge states observed have higher charge than the theoretical maximal charge on spherical globular protein, as determined by the De La Mora relationship (ZR = 0.0778m; for the EncFtnsH monomer ZR = 8.9) Fernandez.	FIG
+211	218	monomer	oligomeric_state	In addition, many of the charge states observed have higher charge than the theoretical maximal charge on spherical globular protein, as determined by the De La Mora relationship (ZR = 0.0778m; for the EncFtnsH monomer ZR = 8.9) Fernandez.	FIG
+219	221	ZR	evidence	In addition, many of the charge states observed have higher charge than the theoretical maximal charge on spherical globular protein, as determined by the De La Mora relationship (ZR = 0.0778m; for the EncFtnsH monomer ZR = 8.9) Fernandez.	FIG
+72	82	disordered	protein_state	As described by Beveridge et al., all these factors are indicative of a disordered protein.	FIG
+29	33	holo	protein_state	Gas-phase disassembly of the holo-EncFtnsH decameric assembly.	FIG
+34	42	EncFtnsH	protein	Gas-phase disassembly of the holo-EncFtnsH decameric assembly.	FIG
+43	52	decameric	oligomeric_state	Gas-phase disassembly of the holo-EncFtnsH decameric assembly.	FIG
+11	23	charge state	evidence	The entire charge state distribution of the Fe-loaded holo- EncFtnsH assembly (green circles) was subject to collisional-induced dissociation (CID) by increasing the source cone voltage to 200 V and the trap voltage to 50 V. The resulting CID mass spectrum (A) revealed that dissociation of the holo- EncFtnsH decamer primarily occurred via ejection of a highly charged monomer (blue circles), leaving the ‘stripped’ complex (a 9mer; 118.7 kDa; yellow circles).	FIG
+44	53	Fe-loaded	protein_state	The entire charge state distribution of the Fe-loaded holo- EncFtnsH assembly (green circles) was subject to collisional-induced dissociation (CID) by increasing the source cone voltage to 200 V and the trap voltage to 50 V. The resulting CID mass spectrum (A) revealed that dissociation of the holo- EncFtnsH decamer primarily occurred via ejection of a highly charged monomer (blue circles), leaving the ‘stripped’ complex (a 9mer; 118.7 kDa; yellow circles).	FIG
+54	58	holo	protein_state	The entire charge state distribution of the Fe-loaded holo- EncFtnsH assembly (green circles) was subject to collisional-induced dissociation (CID) by increasing the source cone voltage to 200 V and the trap voltage to 50 V. The resulting CID mass spectrum (A) revealed that dissociation of the holo- EncFtnsH decamer primarily occurred via ejection of a highly charged monomer (blue circles), leaving the ‘stripped’ complex (a 9mer; 118.7 kDa; yellow circles).	FIG
+60	68	EncFtnsH	protein	The entire charge state distribution of the Fe-loaded holo- EncFtnsH assembly (green circles) was subject to collisional-induced dissociation (CID) by increasing the source cone voltage to 200 V and the trap voltage to 50 V. The resulting CID mass spectrum (A) revealed that dissociation of the holo- EncFtnsH decamer primarily occurred via ejection of a highly charged monomer (blue circles), leaving the ‘stripped’ complex (a 9mer; 118.7 kDa; yellow circles).	FIG
+109	141	collisional-induced dissociation	experimental_method	The entire charge state distribution of the Fe-loaded holo- EncFtnsH assembly (green circles) was subject to collisional-induced dissociation (CID) by increasing the source cone voltage to 200 V and the trap voltage to 50 V. The resulting CID mass spectrum (A) revealed that dissociation of the holo- EncFtnsH decamer primarily occurred via ejection of a highly charged monomer (blue circles), leaving the ‘stripped’ complex (a 9mer; 118.7 kDa; yellow circles).	FIG
+143	146	CID	experimental_method	The entire charge state distribution of the Fe-loaded holo- EncFtnsH assembly (green circles) was subject to collisional-induced dissociation (CID) by increasing the source cone voltage to 200 V and the trap voltage to 50 V. The resulting CID mass spectrum (A) revealed that dissociation of the holo- EncFtnsH decamer primarily occurred via ejection of a highly charged monomer (blue circles), leaving the ‘stripped’ complex (a 9mer; 118.7 kDa; yellow circles).	FIG
+239	242	CID	experimental_method	The entire charge state distribution of the Fe-loaded holo- EncFtnsH assembly (green circles) was subject to collisional-induced dissociation (CID) by increasing the source cone voltage to 200 V and the trap voltage to 50 V. The resulting CID mass spectrum (A) revealed that dissociation of the holo- EncFtnsH decamer primarily occurred via ejection of a highly charged monomer (blue circles), leaving the ‘stripped’ complex (a 9mer; 118.7 kDa; yellow circles).	FIG
+243	256	mass spectrum	evidence	The entire charge state distribution of the Fe-loaded holo- EncFtnsH assembly (green circles) was subject to collisional-induced dissociation (CID) by increasing the source cone voltage to 200 V and the trap voltage to 50 V. The resulting CID mass spectrum (A) revealed that dissociation of the holo- EncFtnsH decamer primarily occurred via ejection of a highly charged monomer (blue circles), leaving the ‘stripped’ complex (a 9mer; 118.7 kDa; yellow circles).	FIG
+295	299	holo	protein_state	The entire charge state distribution of the Fe-loaded holo- EncFtnsH assembly (green circles) was subject to collisional-induced dissociation (CID) by increasing the source cone voltage to 200 V and the trap voltage to 50 V. The resulting CID mass spectrum (A) revealed that dissociation of the holo- EncFtnsH decamer primarily occurred via ejection of a highly charged monomer (blue circles), leaving the ‘stripped’ complex (a 9mer; 118.7 kDa; yellow circles).	FIG
+301	309	EncFtnsH	protein	The entire charge state distribution of the Fe-loaded holo- EncFtnsH assembly (green circles) was subject to collisional-induced dissociation (CID) by increasing the source cone voltage to 200 V and the trap voltage to 50 V. The resulting CID mass spectrum (A) revealed that dissociation of the holo- EncFtnsH decamer primarily occurred via ejection of a highly charged monomer (blue circles), leaving the ‘stripped’ complex (a 9mer; 118.7 kDa; yellow circles).	FIG
+310	317	decamer	oligomeric_state	The entire charge state distribution of the Fe-loaded holo- EncFtnsH assembly (green circles) was subject to collisional-induced dissociation (CID) by increasing the source cone voltage to 200 V and the trap voltage to 50 V. The resulting CID mass spectrum (A) revealed that dissociation of the holo- EncFtnsH decamer primarily occurred via ejection of a highly charged monomer (blue circles), leaving the ‘stripped’ complex (a 9mer; 118.7 kDa; yellow circles).	FIG
+370	377	monomer	oligomeric_state	The entire charge state distribution of the Fe-loaded holo- EncFtnsH assembly (green circles) was subject to collisional-induced dissociation (CID) by increasing the source cone voltage to 200 V and the trap voltage to 50 V. The resulting CID mass spectrum (A) revealed that dissociation of the holo- EncFtnsH decamer primarily occurred via ejection of a highly charged monomer (blue circles), leaving the ‘stripped’ complex (a 9mer; 118.7 kDa; yellow circles).	FIG
+407	415	stripped	protein_state	The entire charge state distribution of the Fe-loaded holo- EncFtnsH assembly (green circles) was subject to collisional-induced dissociation (CID) by increasing the source cone voltage to 200 V and the trap voltage to 50 V. The resulting CID mass spectrum (A) revealed that dissociation of the holo- EncFtnsH decamer primarily occurred via ejection of a highly charged monomer (blue circles), leaving the ‘stripped’ complex (a 9mer; 118.7 kDa; yellow circles).	FIG
+428	432	9mer	oligomeric_state	The entire charge state distribution of the Fe-loaded holo- EncFtnsH assembly (green circles) was subject to collisional-induced dissociation (CID) by increasing the source cone voltage to 200 V and the trap voltage to 50 V. The resulting CID mass spectrum (A) revealed that dissociation of the holo- EncFtnsH decamer primarily occurred via ejection of a highly charged monomer (blue circles), leaving the ‘stripped’ complex (a 9mer; 118.7 kDa; yellow circles).	FIG
+24	31	monomer	oligomeric_state	The mass of the ejected-monomer is consistent with apo- EncFtnsH (13.2 kDa), suggesting unfolding of the monomer (and loss of Fe) occurs during ejection from the complex.	FIG
+51	54	apo	protein_state	The mass of the ejected-monomer is consistent with apo- EncFtnsH (13.2 kDa), suggesting unfolding of the monomer (and loss of Fe) occurs during ejection from the complex.	FIG
+56	64	EncFtnsH	protein	The mass of the ejected-monomer is consistent with apo- EncFtnsH (13.2 kDa), suggesting unfolding of the monomer (and loss of Fe) occurs during ejection from the complex.	FIG
+105	112	monomer	oligomeric_state	The mass of the ejected-monomer is consistent with apo- EncFtnsH (13.2 kDa), suggesting unfolding of the monomer (and loss of Fe) occurs during ejection from the complex.	FIG
+118	125	loss of	protein_state	The mass of the ejected-monomer is consistent with apo- EncFtnsH (13.2 kDa), suggesting unfolding of the monomer (and loss of Fe) occurs during ejection from the complex.	FIG
+126	128	Fe	chemical	The mass of the ejected-monomer is consistent with apo- EncFtnsH (13.2 kDa), suggesting unfolding of the monomer (and loss of Fe) occurs during ejection from the complex.	FIG
+194	197	CID	experimental_method	This observation of asymmetric charge partitioning of the sub-complexes with respect to the mass of the complex is consistent with the 'typical' pathway of dissociation of protein assemblies by CID, as described by.	FIG
+39	51	charge state	evidence	In addition, a third, lower abundance, charge state distribution is observed which overlaps the EncFtn ejected monomer charge state distribution; this region of the spectrum is highlighted in (B).	FIG
+96	102	EncFtn	protein	In addition, a third, lower abundance, charge state distribution is observed which overlaps the EncFtn ejected monomer charge state distribution; this region of the spectrum is highlighted in (B).	FIG
+111	118	monomer	oligomeric_state	In addition, a third, lower abundance, charge state distribution is observed which overlaps the EncFtn ejected monomer charge state distribution; this region of the spectrum is highlighted in (B).	FIG
+119	131	charge state	evidence	In addition, a third, lower abundance, charge state distribution is observed which overlaps the EncFtn ejected monomer charge state distribution; this region of the spectrum is highlighted in (B).	FIG
+48	56	EncFtnsH	protein	This distribution is consistent with an ejected EncFtnsH dimer (orange circles).	FIG
+57	62	dimer	oligomeric_state	This distribution is consistent with an ejected EncFtnsH dimer (orange circles).	FIG
+49	61	charge state	evidence	Interestingly, closer analysis of the individual charge state of this dimeric CID product shows that this sub-complex exists in three forms – displaying mass consistent with an EncFtnsH dimer binding 0, 1, and 2 Fe ions.	FIG
+70	77	dimeric	oligomeric_state	Interestingly, closer analysis of the individual charge state of this dimeric CID product shows that this sub-complex exists in three forms – displaying mass consistent with an EncFtnsH dimer binding 0, 1, and 2 Fe ions.	FIG
+78	81	CID	experimental_method	Interestingly, closer analysis of the individual charge state of this dimeric CID product shows that this sub-complex exists in three forms – displaying mass consistent with an EncFtnsH dimer binding 0, 1, and 2 Fe ions.	FIG
+177	185	EncFtnsH	protein	Interestingly, closer analysis of the individual charge state of this dimeric CID product shows that this sub-complex exists in three forms – displaying mass consistent with an EncFtnsH dimer binding 0, 1, and 2 Fe ions.	FIG
+186	191	dimer	oligomeric_state	Interestingly, closer analysis of the individual charge state of this dimeric CID product shows that this sub-complex exists in three forms – displaying mass consistent with an EncFtnsH dimer binding 0, 1, and 2 Fe ions.	FIG
+212	214	Fe	chemical	Interestingly, closer analysis of the individual charge state of this dimeric CID product shows that this sub-complex exists in three forms – displaying mass consistent with an EncFtnsH dimer binding 0, 1, and 2 Fe ions.	FIG
+42	54	charge state	evidence	This is highlighted in (C), where the 15+ charge state of the EncFtnsH dimer is shown; 3 peaks are observed with m/z 1760.5, 1763.8, and 1767.0 Th – the lowest peak corresponds to neutral masses of 26392.5 Da [predicted EncFtnsH dimer, (C572H884N172O185S2)2; 26388.6 Da].	FIG
+62	70	EncFtnsH	protein	This is highlighted in (C), where the 15+ charge state of the EncFtnsH dimer is shown; 3 peaks are observed with m/z 1760.5, 1763.8, and 1767.0 Th – the lowest peak corresponds to neutral masses of 26392.5 Da [predicted EncFtnsH dimer, (C572H884N172O185S2)2; 26388.6 Da].	FIG
+71	76	dimer	oligomeric_state	This is highlighted in (C), where the 15+ charge state of the EncFtnsH dimer is shown; 3 peaks are observed with m/z 1760.5, 1763.8, and 1767.0 Th – the lowest peak corresponds to neutral masses of 26392.5 Da [predicted EncFtnsH dimer, (C572H884N172O185S2)2; 26388.6 Da].	FIG
+89	94	peaks	evidence	This is highlighted in (C), where the 15+ charge state of the EncFtnsH dimer is shown; 3 peaks are observed with m/z 1760.5, 1763.8, and 1767.0 Th – the lowest peak corresponds to neutral masses of 26392.5 Da [predicted EncFtnsH dimer, (C572H884N172O185S2)2; 26388.6 Da].	FIG
+220	228	EncFtnsH	protein	This is highlighted in (C), where the 15+ charge state of the EncFtnsH dimer is shown; 3 peaks are observed with m/z 1760.5, 1763.8, and 1767.0 Th – the lowest peak corresponds to neutral masses of 26392.5 Da [predicted EncFtnsH dimer, (C572H884N172O185S2)2; 26388.6 Da].	FIG
+229	234	dimer	oligomeric_state	This is highlighted in (C), where the 15+ charge state of the EncFtnsH dimer is shown; 3 peaks are observed with m/z 1760.5, 1763.8, and 1767.0 Th – the lowest peak corresponds to neutral masses of 26392.5 Da [predicted EncFtnsH dimer, (C572H884N172O185S2)2; 26388.6 Da].	FIG
+16	21	peaks	evidence	The two further peaks have a delta-mass of ~+50 Da, consistent with Fe binding.	FIG
+68	70	Fe	chemical	The two further peaks have a delta-mass of ~+50 Da, consistent with Fe binding.	FIG
+54	57	CID	experimental_method	We interpret these observations as partial ‘atypical’ CID fragmentation of the decameric complex – i.e. fragmentation of the initial complex with retention of subunit and ligand interactions.	FIG
+79	88	decameric	oligomeric_state	We interpret these observations as partial ‘atypical’ CID fragmentation of the decameric complex – i.e. fragmentation of the initial complex with retention of subunit and ligand interactions.	FIG
+40	50	iron-bound	protein_state	We postulate the high stability of this iron-bound dimer sub-complex is due to the metal coordination at the dimer interface, increasing the strength of the dimer interface.	FIG
+51	56	dimer	oligomeric_state	We postulate the high stability of this iron-bound dimer sub-complex is due to the metal coordination at the dimer interface, increasing the strength of the dimer interface.	FIG
+83	88	metal	chemical	We postulate the high stability of this iron-bound dimer sub-complex is due to the metal coordination at the dimer interface, increasing the strength of the dimer interface.	FIG
+89	101	coordination	bond_interaction	We postulate the high stability of this iron-bound dimer sub-complex is due to the metal coordination at the dimer interface, increasing the strength of the dimer interface.	FIG
+109	124	dimer interface	site	We postulate the high stability of this iron-bound dimer sub-complex is due to the metal coordination at the dimer interface, increasing the strength of the dimer interface.	FIG
+157	172	dimer interface	site	We postulate the high stability of this iron-bound dimer sub-complex is due to the metal coordination at the dimer interface, increasing the strength of the dimer interface.	FIG
+81	90	decameric	oligomeric_state	Taken together, these observations support our findings that the topology of the decameric EncFtnsH assembly is arranged as a pentamer of dimers, with two Fe ions at each dimer interface.	FIG
+91	99	EncFtnsH	protein	Taken together, these observations support our findings that the topology of the decameric EncFtnsH assembly is arranged as a pentamer of dimers, with two Fe ions at each dimer interface.	FIG
+126	134	pentamer	oligomeric_state	Taken together, these observations support our findings that the topology of the decameric EncFtnsH assembly is arranged as a pentamer of dimers, with two Fe ions at each dimer interface.	FIG
+138	144	dimers	oligomeric_state	Taken together, these observations support our findings that the topology of the decameric EncFtnsH assembly is arranged as a pentamer of dimers, with two Fe ions at each dimer interface.	FIG
+155	157	Fe	chemical	Taken together, these observations support our findings that the topology of the decameric EncFtnsH assembly is arranged as a pentamer of dimers, with two Fe ions at each dimer interface.	FIG
+171	186	dimer interface	site	Taken together, these observations support our findings that the topology of the decameric EncFtnsH assembly is arranged as a pentamer of dimers, with two Fe ions at each dimer interface.	FIG
+0	24	Native mass spectrometry	experimental_method	Native mass spectrometry and ion mobility analysis of iron loading in EncFtnsH.	FIG
+29	50	ion mobility analysis	experimental_method	Native mass spectrometry and ion mobility analysis of iron loading in EncFtnsH.	FIG
+54	58	iron	chemical	Native mass spectrometry and ion mobility analysis of iron loading in EncFtnsH.	FIG
+70	78	EncFtnsH	protein	Native mass spectrometry and ion mobility analysis of iron loading in EncFtnsH.	FIG
+4	11	spectra	evidence	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Native nanoelectrospray ionization (nESI) mass spectrometry of EncFtnsH at varying iron concentrations.	FIG
+45	52	acetate	chemical	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Native nanoelectrospray ionization (nESI) mass spectrometry of EncFtnsH at varying iron concentrations.	FIG
+103	137	Native nanoelectrospray ionization	experimental_method	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Native nanoelectrospray ionization (nESI) mass spectrometry of EncFtnsH at varying iron concentrations.	FIG
+139	143	nESI	experimental_method	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Native nanoelectrospray ionization (nESI) mass spectrometry of EncFtnsH at varying iron concentrations.	FIG
+145	162	mass spectrometry	experimental_method	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Native nanoelectrospray ionization (nESI) mass spectrometry of EncFtnsH at varying iron concentrations.	FIG
+166	174	EncFtnsH	protein	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Native nanoelectrospray ionization (nESI) mass spectrometry of EncFtnsH at varying iron concentrations.	FIG
+186	190	iron	chemical	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Native nanoelectrospray ionization (nESI) mass spectrometry of EncFtnsH at varying iron concentrations.	FIG
+4	8	nESI	experimental_method	A1, nESI spectrum of iron-free EncFtnsH displays a charge state distribution consistent with EncFtnsH monomer (blue circles, 13,194 Da).	FIG
+9	17	spectrum	evidence	A1, nESI spectrum of iron-free EncFtnsH displays a charge state distribution consistent with EncFtnsH monomer (blue circles, 13,194 Da).	FIG
+21	30	iron-free	protein_state	A1, nESI spectrum of iron-free EncFtnsH displays a charge state distribution consistent with EncFtnsH monomer (blue circles, 13,194 Da).	FIG
+31	39	EncFtnsH	protein	A1, nESI spectrum of iron-free EncFtnsH displays a charge state distribution consistent with EncFtnsH monomer (blue circles, 13,194 Da).	FIG
+51	63	charge state	evidence	A1, nESI spectrum of iron-free EncFtnsH displays a charge state distribution consistent with EncFtnsH monomer (blue circles, 13,194 Da).	FIG
+93	101	EncFtnsH	protein	A1, nESI spectrum of iron-free EncFtnsH displays a charge state distribution consistent with EncFtnsH monomer (blue circles, 13,194 Da).	FIG
+102	109	monomer	oligomeric_state	A1, nESI spectrum of iron-free EncFtnsH displays a charge state distribution consistent with EncFtnsH monomer (blue circles, 13,194 Da).	FIG
+40	44	Fe2+	chemical	Addition of 100 µM (A2) and 300 µM (A3) Fe2+ results in the appearance of a second higher molecular weight charge state distribution consistent with a decameric assembly of EncFtnsH (green circles, 132.6 kDa).	FIG
+90	106	molecular weight	evidence	Addition of 100 µM (A2) and 300 µM (A3) Fe2+ results in the appearance of a second higher molecular weight charge state distribution consistent with a decameric assembly of EncFtnsH (green circles, 132.6 kDa).	FIG
+107	119	charge state	evidence	Addition of 100 µM (A2) and 300 µM (A3) Fe2+ results in the appearance of a second higher molecular weight charge state distribution consistent with a decameric assembly of EncFtnsH (green circles, 132.6 kDa).	FIG
+151	160	decameric	oligomeric_state	Addition of 100 µM (A2) and 300 µM (A3) Fe2+ results in the appearance of a second higher molecular weight charge state distribution consistent with a decameric assembly of EncFtnsH (green circles, 132.6 kDa).	FIG
+173	181	EncFtnsH	protein	Addition of 100 µM (A2) and 300 µM (A3) Fe2+ results in the appearance of a second higher molecular weight charge state distribution consistent with a decameric assembly of EncFtnsH (green circles, 132.6 kDa).	FIG
+4	24	Ion mobility (IM)-MS	experimental_method	(B) Ion mobility (IM)-MS of the iron-bound holo-EncFtnsH decamer.	FIG
+32	42	iron-bound	protein_state	(B) Ion mobility (IM)-MS of the iron-bound holo-EncFtnsH decamer.	FIG
+43	47	holo	protein_state	(B) Ion mobility (IM)-MS of the iron-bound holo-EncFtnsH decamer.	FIG
+48	56	EncFtnsH	protein	(B) Ion mobility (IM)-MS of the iron-bound holo-EncFtnsH decamer.	FIG
+57	64	decamer	oligomeric_state	(B) Ion mobility (IM)-MS of the iron-bound holo-EncFtnsH decamer.	FIG
+5	10	Peaks	evidence	Top, Peaks corresponding to the 22+ to 26+ charge states of a homo-decameric assembly of EncFtnsH are observed (132.6 kDa).	FIG
+43	56	charge states	evidence	Top, Peaks corresponding to the 22+ to 26+ charge states of a homo-decameric assembly of EncFtnsH are observed (132.6 kDa).	FIG
+62	76	homo-decameric	oligomeric_state	Top, Peaks corresponding to the 22+ to 26+ charge states of a homo-decameric assembly of EncFtnsH are observed (132.6 kDa).	FIG
+89	97	EncFtnsH	protein	Top, Peaks corresponding to the 22+ to 26+ charge states of a homo-decameric assembly of EncFtnsH are observed (132.6 kDa).	FIG
+32	44	charge state	evidence	Top Insert, Analysis of the 24+ charge state of the assembly at m/z 5528.2 Th.	FIG
+39	51	charge state	evidence	The theoretical average m/z of the 24+ charge state with no additional metals bound is marked by a red line (5498.7 Th); the observed m/z of the 24+ charge state indicates that the EncFtnsH assembly binds between 10 (green line, 5521.1 Th) and 15 Fe ions (blue line, 5532.4 Th) per decamer.	FIG
+149	161	charge state	evidence	The theoretical average m/z of the 24+ charge state with no additional metals bound is marked by a red line (5498.7 Th); the observed m/z of the 24+ charge state indicates that the EncFtnsH assembly binds between 10 (green line, 5521.1 Th) and 15 Fe ions (blue line, 5532.4 Th) per decamer.	FIG
+181	189	EncFtnsH	protein	The theoretical average m/z of the 24+ charge state with no additional metals bound is marked by a red line (5498.7 Th); the observed m/z of the 24+ charge state indicates that the EncFtnsH assembly binds between 10 (green line, 5521.1 Th) and 15 Fe ions (blue line, 5532.4 Th) per decamer.	FIG
+247	249	Fe	chemical	The theoretical average m/z of the 24+ charge state with no additional metals bound is marked by a red line (5498.7 Th); the observed m/z of the 24+ charge state indicates that the EncFtnsH assembly binds between 10 (green line, 5521.1 Th) and 15 Fe ions (blue line, 5532.4 Th) per decamer.	FIG
+282	289	decamer	oligomeric_state	The theoretical average m/z of the 24+ charge state with no additional metals bound is marked by a red line (5498.7 Th); the observed m/z of the 24+ charge state indicates that the EncFtnsH assembly binds between 10 (green line, 5521.1 Th) and 15 Fe ions (blue line, 5532.4 Th) per decamer.	FIG
+12	38	arrival time distributions	evidence	Bottom, The arrival time distributions (ion mobility data) of all ions in the EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale).	FIG
+40	57	ion mobility data	evidence	Bottom, The arrival time distributions (ion mobility data) of all ions in the EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale).	FIG
+78	86	EncFtnsH	protein	Bottom, The arrival time distributions (ion mobility data) of all ions in the EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale).	FIG
+87	99	charge state	evidence	Bottom, The arrival time distributions (ion mobility data) of all ions in the EncFtnsH charge state distribution displayed as a greyscale heat map (linear intensity scale).	FIG
+18	43	arrival time distribution	evidence	Bottom right, The arrival time distribution of the 24+ charge state (dashed blue box) has been extracted and plotted.	FIG
+55	67	charge state	evidence	Bottom right, The arrival time distribution of the 24+ charge state (dashed blue box) has been extracted and plotted.	FIG
+4	14	drift time	evidence	The drift time for this ion is shown (ms), along with the calibrated collision cross section (CCS), Ω (nm2).	FIG
+69	92	collision cross section	evidence	The drift time for this ion is shown (ms), along with the calibrated collision cross section (CCS), Ω (nm2).	FIG
+94	97	CCS	evidence	The drift time for this ion is shown (ms), along with the calibrated collision cross section (CCS), Ω (nm2).	FIG
+100	101	Ω	evidence	The drift time for this ion is shown (ms), along with the calibrated collision cross section (CCS), Ω (nm2).	FIG
+62	70	EncFtnsH	protein	In order to confirm the assignment of the oligomeric state of EncFtnsH and investigate further the Fe2+-dependent assembly, we used native nano-electrospray ionization (nESI) and ion-mobility mass spectrometry (IM-MS).	RESULTS
+99	103	Fe2+	chemical	In order to confirm the assignment of the oligomeric state of EncFtnsH and investigate further the Fe2+-dependent assembly, we used native nano-electrospray ionization (nESI) and ion-mobility mass spectrometry (IM-MS).	RESULTS
+132	167	native nano-electrospray ionization	experimental_method	In order to confirm the assignment of the oligomeric state of EncFtnsH and investigate further the Fe2+-dependent assembly, we used native nano-electrospray ionization (nESI) and ion-mobility mass spectrometry (IM-MS).	RESULTS
+169	173	nESI	experimental_method	In order to confirm the assignment of the oligomeric state of EncFtnsH and investigate further the Fe2+-dependent assembly, we used native nano-electrospray ionization (nESI) and ion-mobility mass spectrometry (IM-MS).	RESULTS
+179	209	ion-mobility mass spectrometry	experimental_method	In order to confirm the assignment of the oligomeric state of EncFtnsH and investigate further the Fe2+-dependent assembly, we used native nano-electrospray ionization (nESI) and ion-mobility mass spectrometry (IM-MS).	RESULTS
+211	216	IM-MS	experimental_method	In order to confirm the assignment of the oligomeric state of EncFtnsH and investigate further the Fe2+-dependent assembly, we used native nano-electrospray ionization (nESI) and ion-mobility mass spectrometry (IM-MS).	RESULTS
+23	45	recombinant production	experimental_method	As described above, by recombinant production of EncFtnsH in minimal media we were able to limit the bioavailability of iron.	RESULTS
+49	57	EncFtnsH	protein	As described above, by recombinant production of EncFtnsH in minimal media we were able to limit the bioavailability of iron.	RESULTS
+120	124	iron	chemical	As described above, by recombinant production of EncFtnsH in minimal media we were able to limit the bioavailability of iron.	RESULTS
+0	9	Native MS	experimental_method	Native MS analysis of EncFtnsH produced in this way displayed a charge state distribution consistent with an EncFtnsH monomer (blue circles, Figure 7A1) with an average neutral mass of 13,194 Da, in agreement with the predicted mass of the EncFtnsH protein (13,194.53 Da).	RESULTS
+22	30	EncFtnsH	protein	Native MS analysis of EncFtnsH produced in this way displayed a charge state distribution consistent with an EncFtnsH monomer (blue circles, Figure 7A1) with an average neutral mass of 13,194 Da, in agreement with the predicted mass of the EncFtnsH protein (13,194.53 Da).	RESULTS
+64	76	charge state	evidence	Native MS analysis of EncFtnsH produced in this way displayed a charge state distribution consistent with an EncFtnsH monomer (blue circles, Figure 7A1) with an average neutral mass of 13,194 Da, in agreement with the predicted mass of the EncFtnsH protein (13,194.53 Da).	RESULTS
+109	117	EncFtnsH	protein	Native MS analysis of EncFtnsH produced in this way displayed a charge state distribution consistent with an EncFtnsH monomer (blue circles, Figure 7A1) with an average neutral mass of 13,194 Da, in agreement with the predicted mass of the EncFtnsH protein (13,194.53 Da).	RESULTS
+118	125	monomer	oligomeric_state	Native MS analysis of EncFtnsH produced in this way displayed a charge state distribution consistent with an EncFtnsH monomer (blue circles, Figure 7A1) with an average neutral mass of 13,194 Da, in agreement with the predicted mass of the EncFtnsH protein (13,194.53 Da).	RESULTS
+240	248	EncFtnsH	protein	Native MS analysis of EncFtnsH produced in this way displayed a charge state distribution consistent with an EncFtnsH monomer (blue circles, Figure 7A1) with an average neutral mass of 13,194 Da, in agreement with the predicted mass of the EncFtnsH protein (13,194.53 Da).	RESULTS
+0	9	Titration	experimental_method	Titration with Fe2+ directly before native MS analysis resulted in the appearance of a new charge state distribution, consistent with an EncFtnsH decameric assembly (+22 to +26; 132.65 kDa) (Figure 7A2/3).	RESULTS
+15	19	Fe2+	chemical	Titration with Fe2+ directly before native MS analysis resulted in the appearance of a new charge state distribution, consistent with an EncFtnsH decameric assembly (+22 to +26; 132.65 kDa) (Figure 7A2/3).	RESULTS
+36	45	native MS	experimental_method	Titration with Fe2+ directly before native MS analysis resulted in the appearance of a new charge state distribution, consistent with an EncFtnsH decameric assembly (+22 to +26; 132.65 kDa) (Figure 7A2/3).	RESULTS
+91	103	charge state	evidence	Titration with Fe2+ directly before native MS analysis resulted in the appearance of a new charge state distribution, consistent with an EncFtnsH decameric assembly (+22 to +26; 132.65 kDa) (Figure 7A2/3).	RESULTS
+137	145	EncFtnsH	protein	Titration with Fe2+ directly before native MS analysis resulted in the appearance of a new charge state distribution, consistent with an EncFtnsH decameric assembly (+22 to +26; 132.65 kDa) (Figure 7A2/3).	RESULTS
+146	155	decameric	oligomeric_state	Titration with Fe2+ directly before native MS analysis resulted in the appearance of a new charge state distribution, consistent with an EncFtnsH decameric assembly (+22 to +26; 132.65 kDa) (Figure 7A2/3).	RESULTS
+90	94	iron	chemical	After instrument optimization, the mass resolving power achieved was sufficient to assign iron-loading in the complex to between 10 and 15 Fe ions per decamer (Figure 7B, inset top right), consistent with the presence of 10 irons in the FOC and the coordination of iron in the Glu31/34-site occupied by calcium in the crystal structure (Δmass observed ~0.67 kDa).	RESULTS
+139	141	Fe	chemical	After instrument optimization, the mass resolving power achieved was sufficient to assign iron-loading in the complex to between 10 and 15 Fe ions per decamer (Figure 7B, inset top right), consistent with the presence of 10 irons in the FOC and the coordination of iron in the Glu31/34-site occupied by calcium in the crystal structure (Δmass observed ~0.67 kDa).	RESULTS
+151	158	decamer	oligomeric_state	After instrument optimization, the mass resolving power achieved was sufficient to assign iron-loading in the complex to between 10 and 15 Fe ions per decamer (Figure 7B, inset top right), consistent with the presence of 10 irons in the FOC and the coordination of iron in the Glu31/34-site occupied by calcium in the crystal structure (Δmass observed ~0.67 kDa).	RESULTS
+209	220	presence of	protein_state	After instrument optimization, the mass resolving power achieved was sufficient to assign iron-loading in the complex to between 10 and 15 Fe ions per decamer (Figure 7B, inset top right), consistent with the presence of 10 irons in the FOC and the coordination of iron in the Glu31/34-site occupied by calcium in the crystal structure (Δmass observed ~0.67 kDa).	RESULTS
+224	229	irons	chemical	After instrument optimization, the mass resolving power achieved was sufficient to assign iron-loading in the complex to between 10 and 15 Fe ions per decamer (Figure 7B, inset top right), consistent with the presence of 10 irons in the FOC and the coordination of iron in the Glu31/34-site occupied by calcium in the crystal structure (Δmass observed ~0.67 kDa).	RESULTS
+237	240	FOC	site	After instrument optimization, the mass resolving power achieved was sufficient to assign iron-loading in the complex to between 10 and 15 Fe ions per decamer (Figure 7B, inset top right), consistent with the presence of 10 irons in the FOC and the coordination of iron in the Glu31/34-site occupied by calcium in the crystal structure (Δmass observed ~0.67 kDa).	RESULTS
+249	261	coordination	bond_interaction	After instrument optimization, the mass resolving power achieved was sufficient to assign iron-loading in the complex to between 10 and 15 Fe ions per decamer (Figure 7B, inset top right), consistent with the presence of 10 irons in the FOC and the coordination of iron in the Glu31/34-site occupied by calcium in the crystal structure (Δmass observed ~0.67 kDa).	RESULTS
+265	269	iron	chemical	After instrument optimization, the mass resolving power achieved was sufficient to assign iron-loading in the complex to between 10 and 15 Fe ions per decamer (Figure 7B, inset top right), consistent with the presence of 10 irons in the FOC and the coordination of iron in the Glu31/34-site occupied by calcium in the crystal structure (Δmass observed ~0.67 kDa).	RESULTS
+277	290	Glu31/34-site	site	After instrument optimization, the mass resolving power achieved was sufficient to assign iron-loading in the complex to between 10 and 15 Fe ions per decamer (Figure 7B, inset top right), consistent with the presence of 10 irons in the FOC and the coordination of iron in the Glu31/34-site occupied by calcium in the crystal structure (Δmass observed ~0.67 kDa).	RESULTS
+303	310	calcium	chemical	After instrument optimization, the mass resolving power achieved was sufficient to assign iron-loading in the complex to between 10 and 15 Fe ions per decamer (Figure 7B, inset top right), consistent with the presence of 10 irons in the FOC and the coordination of iron in the Glu31/34-site occupied by calcium in the crystal structure (Δmass observed ~0.67 kDa).	RESULTS
+318	335	crystal structure	evidence	After instrument optimization, the mass resolving power achieved was sufficient to assign iron-loading in the complex to between 10 and 15 Fe ions per decamer (Figure 7B, inset top right), consistent with the presence of 10 irons in the FOC and the coordination of iron in the Glu31/34-site occupied by calcium in the crystal structure (Δmass observed ~0.67 kDa).	RESULTS
+337	342	Δmass	evidence	After instrument optimization, the mass resolving power achieved was sufficient to assign iron-loading in the complex to between 10 and 15 Fe ions per decamer (Figure 7B, inset top right), consistent with the presence of 10 irons in the FOC and the coordination of iron in the Glu31/34-site occupied by calcium in the crystal structure (Δmass observed ~0.67 kDa).	RESULTS
+0	2	MS	experimental_method	MS analysis of EncFtnsH after addition of further Fe2+ did not result in iron loading above this stoichiometry.	RESULTS
+15	23	EncFtnsH	protein	MS analysis of EncFtnsH after addition of further Fe2+ did not result in iron loading above this stoichiometry.	RESULTS
+50	54	Fe2+	chemical	MS analysis of EncFtnsH after addition of further Fe2+ did not result in iron loading above this stoichiometry.	RESULTS
+73	77	iron	chemical	MS analysis of EncFtnsH after addition of further Fe2+ did not result in iron loading above this stoichiometry.	RESULTS
+25	29	iron	chemical	Therefore, the extent of iron binding seen is limited to the FOC and Glu31/34 secondary metal binding site.	RESULTS
+61	64	FOC	site	Therefore, the extent of iron binding seen is limited to the FOC and Glu31/34 secondary metal binding site.	RESULTS
+69	106	Glu31/34 secondary metal binding site	site	Therefore, the extent of iron binding seen is limited to the FOC and Glu31/34 secondary metal binding site.	RESULTS
+28	37	decameric	oligomeric_state	These data suggest that the decameric assembly of EncFtnsH does not accrue iron in the same manner as classical ferritin, which is able to sequester around 4500 iron ions within its nanocage.	RESULTS
+50	58	EncFtnsH	protein	These data suggest that the decameric assembly of EncFtnsH does not accrue iron in the same manner as classical ferritin, which is able to sequester around 4500 iron ions within its nanocage.	RESULTS
+75	79	iron	chemical	These data suggest that the decameric assembly of EncFtnsH does not accrue iron in the same manner as classical ferritin, which is able to sequester around 4500 iron ions within its nanocage.	RESULTS
+102	111	classical	protein_state	These data suggest that the decameric assembly of EncFtnsH does not accrue iron in the same manner as classical ferritin, which is able to sequester around 4500 iron ions within its nanocage.	RESULTS
+112	120	ferritin	protein_type	These data suggest that the decameric assembly of EncFtnsH does not accrue iron in the same manner as classical ferritin, which is able to sequester around 4500 iron ions within its nanocage.	RESULTS
+161	165	iron	chemical	These data suggest that the decameric assembly of EncFtnsH does not accrue iron in the same manner as classical ferritin, which is able to sequester around 4500 iron ions within its nanocage.	RESULTS
+182	190	nanocage	complex_assembly	These data suggest that the decameric assembly of EncFtnsH does not accrue iron in the same manner as classical ferritin, which is able to sequester around 4500 iron ions within its nanocage.	RESULTS
+0	21	Ion mobility analysis	experimental_method	Ion mobility analysis of the EncFtnsH decameric assembly, collected with minimal collisional activation, suggested that it consists of a single conformation with a collision cross section (CCS) of 58.2 nm2 (Figure 7B).	RESULTS
+29	37	EncFtnsH	protein	Ion mobility analysis of the EncFtnsH decameric assembly, collected with minimal collisional activation, suggested that it consists of a single conformation with a collision cross section (CCS) of 58.2 nm2 (Figure 7B).	RESULTS
+38	47	decameric	oligomeric_state	Ion mobility analysis of the EncFtnsH decameric assembly, collected with minimal collisional activation, suggested that it consists of a single conformation with a collision cross section (CCS) of 58.2 nm2 (Figure 7B).	RESULTS
+164	187	collision cross section	evidence	Ion mobility analysis of the EncFtnsH decameric assembly, collected with minimal collisional activation, suggested that it consists of a single conformation with a collision cross section (CCS) of 58.2 nm2 (Figure 7B).	RESULTS
+189	192	CCS	evidence	Ion mobility analysis of the EncFtnsH decameric assembly, collected with minimal collisional activation, suggested that it consists of a single conformation with a collision cross section (CCS) of 58.2 nm2 (Figure 7B).	RESULTS
+53	56	CCS	evidence	This observation is in agreement with the calculated CCS of 58.7 nm2derived from our crystal structure of the EncFtnsH decamer.	RESULTS
+85	102	crystal structure	evidence	This observation is in agreement with the calculated CCS of 58.7 nm2derived from our crystal structure of the EncFtnsH decamer.	RESULTS
+110	118	EncFtnsH	protein	This observation is in agreement with the calculated CCS of 58.7 nm2derived from our crystal structure of the EncFtnsH decamer.	RESULTS
+119	126	decamer	oligomeric_state	This observation is in agreement with the calculated CCS of 58.7 nm2derived from our crystal structure of the EncFtnsH decamer.	RESULTS
+13	18	IM-MS	experimental_method	By contrast, IM-MS measurements of the monomeric EncFtnsH at pH 8.0 under the same instrumental conditions revealed that the metal-free protein monomer exists in a wide range of charge states (+6 to +16) and adopts many conformations in the gas phase with collision cross sections ranging from 12 nm2 to 26 nm2 (Figure 7—figure supplement 1).	RESULTS
+39	48	monomeric	oligomeric_state	By contrast, IM-MS measurements of the monomeric EncFtnsH at pH 8.0 under the same instrumental conditions revealed that the metal-free protein monomer exists in a wide range of charge states (+6 to +16) and adopts many conformations in the gas phase with collision cross sections ranging from 12 nm2 to 26 nm2 (Figure 7—figure supplement 1).	RESULTS
+49	57	EncFtnsH	protein	By contrast, IM-MS measurements of the monomeric EncFtnsH at pH 8.0 under the same instrumental conditions revealed that the metal-free protein monomer exists in a wide range of charge states (+6 to +16) and adopts many conformations in the gas phase with collision cross sections ranging from 12 nm2 to 26 nm2 (Figure 7—figure supplement 1).	RESULTS
+61	67	pH 8.0	protein_state	By contrast, IM-MS measurements of the monomeric EncFtnsH at pH 8.0 under the same instrumental conditions revealed that the metal-free protein monomer exists in a wide range of charge states (+6 to +16) and adopts many conformations in the gas phase with collision cross sections ranging from 12 nm2 to 26 nm2 (Figure 7—figure supplement 1).	RESULTS
+125	135	metal-free	protein_state	By contrast, IM-MS measurements of the monomeric EncFtnsH at pH 8.0 under the same instrumental conditions revealed that the metal-free protein monomer exists in a wide range of charge states (+6 to +16) and adopts many conformations in the gas phase with collision cross sections ranging from 12 nm2 to 26 nm2 (Figure 7—figure supplement 1).	RESULTS
+136	143	protein	protein	By contrast, IM-MS measurements of the monomeric EncFtnsH at pH 8.0 under the same instrumental conditions revealed that the metal-free protein monomer exists in a wide range of charge states (+6 to +16) and adopts many conformations in the gas phase with collision cross sections ranging from 12 nm2 to 26 nm2 (Figure 7—figure supplement 1).	RESULTS
+144	151	monomer	oligomeric_state	By contrast, IM-MS measurements of the monomeric EncFtnsH at pH 8.0 under the same instrumental conditions revealed that the metal-free protein monomer exists in a wide range of charge states (+6 to +16) and adopts many conformations in the gas phase with collision cross sections ranging from 12 nm2 to 26 nm2 (Figure 7—figure supplement 1).	RESULTS
+178	191	charge states	evidence	By contrast, IM-MS measurements of the monomeric EncFtnsH at pH 8.0 under the same instrumental conditions revealed that the metal-free protein monomer exists in a wide range of charge states (+6 to +16) and adopts many conformations in the gas phase with collision cross sections ranging from 12 nm2 to 26 nm2 (Figure 7—figure supplement 1).	RESULTS
+6	11	IM-MS	experimental_method	Thus, IM-MS studies highlight that higher order structure in EncFtnsH is mediated/stabilized by metal binding, an observation that is in agreement with our solution studies.	RESULTS
+61	69	EncFtnsH	protein	Thus, IM-MS studies highlight that higher order structure in EncFtnsH is mediated/stabilized by metal binding, an observation that is in agreement with our solution studies.	RESULTS
+46	50	iron	chemical	Taken together, these results suggest that di-iron binding, forming the FOC in EncFtnsH, is required to stabilize the 4-helix bundle dimer interface, essentially reconstructing the classical ferritin-like fold; once stabilized, these dimers readily associate as pentamers, and the overall assembly adopts the decameric ring arrangement observed in the crystal structure.	RESULTS
+72	75	FOC	site	Taken together, these results suggest that di-iron binding, forming the FOC in EncFtnsH, is required to stabilize the 4-helix bundle dimer interface, essentially reconstructing the classical ferritin-like fold; once stabilized, these dimers readily associate as pentamers, and the overall assembly adopts the decameric ring arrangement observed in the crystal structure.	RESULTS
+79	87	EncFtnsH	protein	Taken together, these results suggest that di-iron binding, forming the FOC in EncFtnsH, is required to stabilize the 4-helix bundle dimer interface, essentially reconstructing the classical ferritin-like fold; once stabilized, these dimers readily associate as pentamers, and the overall assembly adopts the decameric ring arrangement observed in the crystal structure.	RESULTS
+118	132	4-helix bundle	structure_element	Taken together, these results suggest that di-iron binding, forming the FOC in EncFtnsH, is required to stabilize the 4-helix bundle dimer interface, essentially reconstructing the classical ferritin-like fold; once stabilized, these dimers readily associate as pentamers, and the overall assembly adopts the decameric ring arrangement observed in the crystal structure.	RESULTS
+133	148	dimer interface	site	Taken together, these results suggest that di-iron binding, forming the FOC in EncFtnsH, is required to stabilize the 4-helix bundle dimer interface, essentially reconstructing the classical ferritin-like fold; once stabilized, these dimers readily associate as pentamers, and the overall assembly adopts the decameric ring arrangement observed in the crystal structure.	RESULTS
+181	190	classical	protein_state	Taken together, these results suggest that di-iron binding, forming the FOC in EncFtnsH, is required to stabilize the 4-helix bundle dimer interface, essentially reconstructing the classical ferritin-like fold; once stabilized, these dimers readily associate as pentamers, and the overall assembly adopts the decameric ring arrangement observed in the crystal structure.	RESULTS
+191	199	ferritin	protein_type	Taken together, these results suggest that di-iron binding, forming the FOC in EncFtnsH, is required to stabilize the 4-helix bundle dimer interface, essentially reconstructing the classical ferritin-like fold; once stabilized, these dimers readily associate as pentamers, and the overall assembly adopts the decameric ring arrangement observed in the crystal structure.	RESULTS
+234	240	dimers	oligomeric_state	Taken together, these results suggest that di-iron binding, forming the FOC in EncFtnsH, is required to stabilize the 4-helix bundle dimer interface, essentially reconstructing the classical ferritin-like fold; once stabilized, these dimers readily associate as pentamers, and the overall assembly adopts the decameric ring arrangement observed in the crystal structure.	RESULTS
+309	318	decameric	oligomeric_state	Taken together, these results suggest that di-iron binding, forming the FOC in EncFtnsH, is required to stabilize the 4-helix bundle dimer interface, essentially reconstructing the classical ferritin-like fold; once stabilized, these dimers readily associate as pentamers, and the overall assembly adopts the decameric ring arrangement observed in the crystal structure.	RESULTS
+352	369	crystal structure	evidence	Taken together, these results suggest that di-iron binding, forming the FOC in EncFtnsH, is required to stabilize the 4-helix bundle dimer interface, essentially reconstructing the classical ferritin-like fold; once stabilized, these dimers readily associate as pentamers, and the overall assembly adopts the decameric ring arrangement observed in the crystal structure.	RESULTS
+55	64	decameric	oligomeric_state	We subsequently performed gas phase disassembly of the decameric EncFtnsH using collision-induced dissociation (CID) tandem mass spectrometry.	RESULTS
+65	73	EncFtnsH	protein	We subsequently performed gas phase disassembly of the decameric EncFtnsH using collision-induced dissociation (CID) tandem mass spectrometry.	RESULTS
+80	110	collision-induced dissociation	experimental_method	We subsequently performed gas phase disassembly of the decameric EncFtnsH using collision-induced dissociation (CID) tandem mass spectrometry.	RESULTS
+112	115	CID	experimental_method	We subsequently performed gas phase disassembly of the decameric EncFtnsH using collision-induced dissociation (CID) tandem mass spectrometry.	RESULTS
+117	141	tandem mass spectrometry	experimental_method	We subsequently performed gas phase disassembly of the decameric EncFtnsH using collision-induced dissociation (CID) tandem mass spectrometry.	RESULTS
+18	21	CID	experimental_method	Under the correct CID conditions, protein assemblies can dissociate with retention of subunit and ligand interactions, and thus provide structurally-informative evidence as to the topology of the original assembly; this has been termed ‘atypical’ dissociation.	RESULTS
+4	12	EncFtnsH	protein	For EncFtnsH, this atypical dissociation pathway was clearly evident; CID of the EncFtnsH decamer resulted in the appearance of a dimeric EncFtnsH subcomplex containing 0, 1, or 2 iron ions (Figure 7—figure supplement 2).	RESULTS
+70	73	CID	experimental_method	For EncFtnsH, this atypical dissociation pathway was clearly evident; CID of the EncFtnsH decamer resulted in the appearance of a dimeric EncFtnsH subcomplex containing 0, 1, or 2 iron ions (Figure 7—figure supplement 2).	RESULTS
+81	89	EncFtnsH	protein	For EncFtnsH, this atypical dissociation pathway was clearly evident; CID of the EncFtnsH decamer resulted in the appearance of a dimeric EncFtnsH subcomplex containing 0, 1, or 2 iron ions (Figure 7—figure supplement 2).	RESULTS
+90	97	decamer	oligomeric_state	For EncFtnsH, this atypical dissociation pathway was clearly evident; CID of the EncFtnsH decamer resulted in the appearance of a dimeric EncFtnsH subcomplex containing 0, 1, or 2 iron ions (Figure 7—figure supplement 2).	RESULTS
+130	137	dimeric	oligomeric_state	For EncFtnsH, this atypical dissociation pathway was clearly evident; CID of the EncFtnsH decamer resulted in the appearance of a dimeric EncFtnsH subcomplex containing 0, 1, or 2 iron ions (Figure 7—figure supplement 2).	RESULTS
+138	146	EncFtnsH	protein	For EncFtnsH, this atypical dissociation pathway was clearly evident; CID of the EncFtnsH decamer resulted in the appearance of a dimeric EncFtnsH subcomplex containing 0, 1, or 2 iron ions (Figure 7—figure supplement 2).	RESULTS
+180	184	iron	chemical	For EncFtnsH, this atypical dissociation pathway was clearly evident; CID of the EncFtnsH decamer resulted in the appearance of a dimeric EncFtnsH subcomplex containing 0, 1, or 2 iron ions (Figure 7—figure supplement 2).	RESULTS
+16	33	crystal structure	evidence	In light of the crystal structure, this observation can be rationalized as dissociation of the EncFtnsH decamer by disruption of the non-FOC interface with at least partial retention of the FOC interface and the FOC-Fe.	RESULTS
+95	103	EncFtnsH	protein	In light of the crystal structure, this observation can be rationalized as dissociation of the EncFtnsH decamer by disruption of the non-FOC interface with at least partial retention of the FOC interface and the FOC-Fe.	RESULTS
+104	111	decamer	oligomeric_state	In light of the crystal structure, this observation can be rationalized as dissociation of the EncFtnsH decamer by disruption of the non-FOC interface with at least partial retention of the FOC interface and the FOC-Fe.	RESULTS
+133	150	non-FOC interface	site	In light of the crystal structure, this observation can be rationalized as dissociation of the EncFtnsH decamer by disruption of the non-FOC interface with at least partial retention of the FOC interface and the FOC-Fe.	RESULTS
+190	203	FOC interface	site	In light of the crystal structure, this observation can be rationalized as dissociation of the EncFtnsH decamer by disruption of the non-FOC interface with at least partial retention of the FOC interface and the FOC-Fe.	RESULTS
+212	215	FOC	site	In light of the crystal structure, this observation can be rationalized as dissociation of the EncFtnsH decamer by disruption of the non-FOC interface with at least partial retention of the FOC interface and the FOC-Fe.	RESULTS
+216	218	Fe	chemical	In light of the crystal structure, this observation can be rationalized as dissociation of the EncFtnsH decamer by disruption of the non-FOC interface with at least partial retention of the FOC interface and the FOC-Fe.	RESULTS
+95	103	EncFtnsH	protein	Thus, this observation supports our crystallographic assignment of the overall topology of the EncFtnsH assembly as a pentameric assembly of dimers with two iron ions located at the FOC dimer interface.	RESULTS
+118	128	pentameric	oligomeric_state	Thus, this observation supports our crystallographic assignment of the overall topology of the EncFtnsH assembly as a pentameric assembly of dimers with two iron ions located at the FOC dimer interface.	RESULTS
+141	147	dimers	oligomeric_state	Thus, this observation supports our crystallographic assignment of the overall topology of the EncFtnsH assembly as a pentameric assembly of dimers with two iron ions located at the FOC dimer interface.	RESULTS
+157	161	iron	chemical	Thus, this observation supports our crystallographic assignment of the overall topology of the EncFtnsH assembly as a pentameric assembly of dimers with two iron ions located at the FOC dimer interface.	RESULTS
+182	201	FOC dimer interface	site	Thus, this observation supports our crystallographic assignment of the overall topology of the EncFtnsH assembly as a pentameric assembly of dimers with two iron ions located at the FOC dimer interface.	RESULTS
+111	118	crystal	evidence	In addition, this analysis provides evidence that the overall architecture of the complex is consistent in the crystal, solution and gas phases.	RESULTS
+0	11	Ferroxidase	protein_type	Ferroxidase activity	RESULTS
+0	3	TEM	experimental_method	TEM visualization of iron-loaded bacterial nanocompartments and ferritin.	FIG
+21	32	iron-loaded	protein_state	TEM visualization of iron-loaded bacterial nanocompartments and ferritin.	FIG
+33	42	bacterial	taxonomy_domain	TEM visualization of iron-loaded bacterial nanocompartments and ferritin.	FIG
+43	59	nanocompartments	complex_assembly	TEM visualization of iron-loaded bacterial nanocompartments and ferritin.	FIG
+64	72	ferritin	protein_type	TEM visualization of iron-loaded bacterial nanocompartments and ferritin.	FIG
+0	9	Decameric	oligomeric_state	Decameric EncFtnsH, encapsulin, EncFtn-Enc and apoferritin, at 8.5 µM, were mixed with 147 µM, 1 mM, 1 mM and 215 µM acidic Fe(NH4)2(SO4)2, respectively.	FIG
+10	18	EncFtnsH	protein	Decameric EncFtnsH, encapsulin, EncFtn-Enc and apoferritin, at 8.5 µM, were mixed with 147 µM, 1 mM, 1 mM and 215 µM acidic Fe(NH4)2(SO4)2, respectively.	FIG
+20	30	encapsulin	protein	Decameric EncFtnsH, encapsulin, EncFtn-Enc and apoferritin, at 8.5 µM, were mixed with 147 µM, 1 mM, 1 mM and 215 µM acidic Fe(NH4)2(SO4)2, respectively.	FIG
+32	42	EncFtn-Enc	complex_assembly	Decameric EncFtnsH, encapsulin, EncFtn-Enc and apoferritin, at 8.5 µM, were mixed with 147 µM, 1 mM, 1 mM and 215 µM acidic Fe(NH4)2(SO4)2, respectively.	FIG
+47	58	apoferritin	protein_state	Decameric EncFtnsH, encapsulin, EncFtn-Enc and apoferritin, at 8.5 µM, were mixed with 147 µM, 1 mM, 1 mM and 215 µM acidic Fe(NH4)2(SO4)2, respectively.	FIG
+124	138	Fe(NH4)2(SO4)2	chemical	Decameric EncFtnsH, encapsulin, EncFtn-Enc and apoferritin, at 8.5 µM, were mixed with 147 µM, 1 mM, 1 mM and 215 µM acidic Fe(NH4)2(SO4)2, respectively.	FIG
+70	73	TEM	experimental_method	Protein mixtures were incubated at room temperature for 1 hr prior to TEM analysis with or without uranyl acetate stain.	FIG
+99	113	uranyl acetate	chemical	Protein mixtures were incubated at room temperature for 1 hr prior to TEM analysis with or without uranyl acetate stain.	FIG
+16	24	EncFtnsH	protein	(A–D) Unstained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 35,000 x magnification and scale bars indicate 100 nm. (E) Protein-free sample as a control. (F–I) Stained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 140,000 x magnification and scale bars indicate 25 nm.	FIG
+26	36	encapsulin	protein	(A–D) Unstained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 35,000 x magnification and scale bars indicate 100 nm. (E) Protein-free sample as a control. (F–I) Stained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 140,000 x magnification and scale bars indicate 25 nm.	FIG
+38	48	EncFtn-Enc	complex_assembly	(A–D) Unstained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 35,000 x magnification and scale bars indicate 100 nm. (E) Protein-free sample as a control. (F–I) Stained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 140,000 x magnification and scale bars indicate 25 nm.	FIG
+50	61	apoferritin	protein_state	(A–D) Unstained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 35,000 x magnification and scale bars indicate 100 nm. (E) Protein-free sample as a control. (F–I) Stained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 140,000 x magnification and scale bars indicate 25 nm.	FIG
+62	73	loaded with	protein_state	(A–D) Unstained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 35,000 x magnification and scale bars indicate 100 nm. (E) Protein-free sample as a control. (F–I) Stained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 140,000 x magnification and scale bars indicate 25 nm.	FIG
+74	78	Fe2+	chemical	(A–D) Unstained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 35,000 x magnification and scale bars indicate 100 nm. (E) Protein-free sample as a control. (F–I) Stained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 140,000 x magnification and scale bars indicate 25 nm.	FIG
+198	205	Stained	experimental_method	(A–D) Unstained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 35,000 x magnification and scale bars indicate 100 nm. (E) Protein-free sample as a control. (F–I) Stained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 140,000 x magnification and scale bars indicate 25 nm.	FIG
+206	214	EncFtnsH	protein	(A–D) Unstained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 35,000 x magnification and scale bars indicate 100 nm. (E) Protein-free sample as a control. (F–I) Stained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 140,000 x magnification and scale bars indicate 25 nm.	FIG
+216	226	encapsulin	protein	(A–D) Unstained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 35,000 x magnification and scale bars indicate 100 nm. (E) Protein-free sample as a control. (F–I) Stained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 140,000 x magnification and scale bars indicate 25 nm.	FIG
+228	238	EncFtn-Enc	complex_assembly	(A–D) Unstained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 35,000 x magnification and scale bars indicate 100 nm. (E) Protein-free sample as a control. (F–I) Stained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 140,000 x magnification and scale bars indicate 25 nm.	FIG
+240	251	apoferritin	protein_state	(A–D) Unstained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 35,000 x magnification and scale bars indicate 100 nm. (E) Protein-free sample as a control. (F–I) Stained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 140,000 x magnification and scale bars indicate 25 nm.	FIG
+252	263	loaded with	protein_state	(A–D) Unstained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 35,000 x magnification and scale bars indicate 100 nm. (E) Protein-free sample as a control. (F–I) Stained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 140,000 x magnification and scale bars indicate 25 nm.	FIG
+264	268	Fe2+	chemical	(A–D) Unstained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 35,000 x magnification and scale bars indicate 100 nm. (E) Protein-free sample as a control. (F–I) Stained EncFtnsH, encapsulin, EncFtn-Enc, apoferritin loaded with Fe2+, respectively, with 140,000 x magnification and scale bars indicate 25 nm.	FIG
+31	42	ferroxidase	protein_type	Spectroscopic evidence for the ferroxidase activity and comparison of iron loading capacity of apoferritin, EncFtnsH, encapsulin, and EncFtn-Enc.	FIG
+70	74	iron	chemical	Spectroscopic evidence for the ferroxidase activity and comparison of iron loading capacity of apoferritin, EncFtnsH, encapsulin, and EncFtn-Enc.	FIG
+95	106	apoferritin	protein_state	Spectroscopic evidence for the ferroxidase activity and comparison of iron loading capacity of apoferritin, EncFtnsH, encapsulin, and EncFtn-Enc.	FIG
+108	116	EncFtnsH	protein	Spectroscopic evidence for the ferroxidase activity and comparison of iron loading capacity of apoferritin, EncFtnsH, encapsulin, and EncFtn-Enc.	FIG
+118	128	encapsulin	protein	Spectroscopic evidence for the ferroxidase activity and comparison of iron loading capacity of apoferritin, EncFtnsH, encapsulin, and EncFtn-Enc.	FIG
+134	144	EncFtn-Enc	complex_assembly	Spectroscopic evidence for the ferroxidase activity and comparison of iron loading capacity of apoferritin, EncFtnsH, encapsulin, and EncFtn-Enc.	FIG
+4	15	Apoferritin	protein_state	(A) Apoferritin (10 μM monomer concentration) and EncFtnsH decamer fractions (20 μM monomer concentration, 10 μM FOC concentration) were incubated with 20 and 100 μM iron (2 and 10 times molar equivalent Fe2+ per FOC) and progress curves of the oxidation of Fe2+ to Fe3+ at 315 nm were recorded in a spectrophotometer.	FIG
+23	30	monomer	oligomeric_state	(A) Apoferritin (10 μM monomer concentration) and EncFtnsH decamer fractions (20 μM monomer concentration, 10 μM FOC concentration) were incubated with 20 and 100 μM iron (2 and 10 times molar equivalent Fe2+ per FOC) and progress curves of the oxidation of Fe2+ to Fe3+ at 315 nm were recorded in a spectrophotometer.	FIG
+50	58	EncFtnsH	protein	(A) Apoferritin (10 μM monomer concentration) and EncFtnsH decamer fractions (20 μM monomer concentration, 10 μM FOC concentration) were incubated with 20 and 100 μM iron (2 and 10 times molar equivalent Fe2+ per FOC) and progress curves of the oxidation of Fe2+ to Fe3+ at 315 nm were recorded in a spectrophotometer.	FIG
+59	66	decamer	oligomeric_state	(A) Apoferritin (10 μM monomer concentration) and EncFtnsH decamer fractions (20 μM monomer concentration, 10 μM FOC concentration) were incubated with 20 and 100 μM iron (2 and 10 times molar equivalent Fe2+ per FOC) and progress curves of the oxidation of Fe2+ to Fe3+ at 315 nm were recorded in a spectrophotometer.	FIG
+84	91	monomer	oligomeric_state	(A) Apoferritin (10 μM monomer concentration) and EncFtnsH decamer fractions (20 μM monomer concentration, 10 μM FOC concentration) were incubated with 20 and 100 μM iron (2 and 10 times molar equivalent Fe2+ per FOC) and progress curves of the oxidation of Fe2+ to Fe3+ at 315 nm were recorded in a spectrophotometer.	FIG
+113	116	FOC	site	(A) Apoferritin (10 μM monomer concentration) and EncFtnsH decamer fractions (20 μM monomer concentration, 10 μM FOC concentration) were incubated with 20 and 100 μM iron (2 and 10 times molar equivalent Fe2+ per FOC) and progress curves of the oxidation of Fe2+ to Fe3+ at 315 nm were recorded in a spectrophotometer.	FIG
+166	170	iron	chemical	(A) Apoferritin (10 μM monomer concentration) and EncFtnsH decamer fractions (20 μM monomer concentration, 10 μM FOC concentration) were incubated with 20 and 100 μM iron (2 and 10 times molar equivalent Fe2+ per FOC) and progress curves of the oxidation of Fe2+ to Fe3+ at 315 nm were recorded in a spectrophotometer.	FIG
+204	208	Fe2+	chemical	(A) Apoferritin (10 μM monomer concentration) and EncFtnsH decamer fractions (20 μM monomer concentration, 10 μM FOC concentration) were incubated with 20 and 100 μM iron (2 and 10 times molar equivalent Fe2+ per FOC) and progress curves of the oxidation of Fe2+ to Fe3+ at 315 nm were recorded in a spectrophotometer.	FIG
+213	216	FOC	site	(A) Apoferritin (10 μM monomer concentration) and EncFtnsH decamer fractions (20 μM monomer concentration, 10 μM FOC concentration) were incubated with 20 and 100 μM iron (2 and 10 times molar equivalent Fe2+ per FOC) and progress curves of the oxidation of Fe2+ to Fe3+ at 315 nm were recorded in a spectrophotometer.	FIG
+222	237	progress curves	evidence	(A) Apoferritin (10 μM monomer concentration) and EncFtnsH decamer fractions (20 μM monomer concentration, 10 μM FOC concentration) were incubated with 20 and 100 μM iron (2 and 10 times molar equivalent Fe2+ per FOC) and progress curves of the oxidation of Fe2+ to Fe3+ at 315 nm were recorded in a spectrophotometer.	FIG
+258	262	Fe2+	chemical	(A) Apoferritin (10 μM monomer concentration) and EncFtnsH decamer fractions (20 μM monomer concentration, 10 μM FOC concentration) were incubated with 20 and 100 μM iron (2 and 10 times molar equivalent Fe2+ per FOC) and progress curves of the oxidation of Fe2+ to Fe3+ at 315 nm were recorded in a spectrophotometer.	FIG
+266	270	Fe3+	chemical	(A) Apoferritin (10 μM monomer concentration) and EncFtnsH decamer fractions (20 μM monomer concentration, 10 μM FOC concentration) were incubated with 20 and 100 μM iron (2 and 10 times molar equivalent Fe2+ per FOC) and progress curves of the oxidation of Fe2+ to Fe3+ at 315 nm were recorded in a spectrophotometer.	FIG
+28	32	iron	chemical	The background oxidation of iron at 20 and 100 μM in enzyme-free controls are shown for reference. (B) Encapsulin and EncFtn-Enc complexes at 10 μM asymmetric unit concentration were incubated with Fe2+ at 20 and 100 μM and progress curves for iron oxidation at A315 were measured in a UV/visible spectrophotometer.	FIG
+103	113	Encapsulin	protein	The background oxidation of iron at 20 and 100 μM in enzyme-free controls are shown for reference. (B) Encapsulin and EncFtn-Enc complexes at 10 μM asymmetric unit concentration were incubated with Fe2+ at 20 and 100 μM and progress curves for iron oxidation at A315 were measured in a UV/visible spectrophotometer.	FIG
+118	128	EncFtn-Enc	complex_assembly	The background oxidation of iron at 20 and 100 μM in enzyme-free controls are shown for reference. (B) Encapsulin and EncFtn-Enc complexes at 10 μM asymmetric unit concentration were incubated with Fe2+ at 20 and 100 μM and progress curves for iron oxidation at A315 were measured in a UV/visible spectrophotometer.	FIG
+183	192	incubated	experimental_method	The background oxidation of iron at 20 and 100 μM in enzyme-free controls are shown for reference. (B) Encapsulin and EncFtn-Enc complexes at 10 μM asymmetric unit concentration were incubated with Fe2+ at 20 and 100 μM and progress curves for iron oxidation at A315 were measured in a UV/visible spectrophotometer.	FIG
+198	202	Fe2+	chemical	The background oxidation of iron at 20 and 100 μM in enzyme-free controls are shown for reference. (B) Encapsulin and EncFtn-Enc complexes at 10 μM asymmetric unit concentration were incubated with Fe2+ at 20 and 100 μM and progress curves for iron oxidation at A315 were measured in a UV/visible spectrophotometer.	FIG
+224	239	progress curves	evidence	The background oxidation of iron at 20 and 100 μM in enzyme-free controls are shown for reference. (B) Encapsulin and EncFtn-Enc complexes at 10 μM asymmetric unit concentration were incubated with Fe2+ at 20 and 100 μM and progress curves for iron oxidation at A315 were measured in a UV/visible spectrophotometer.	FIG
+244	248	iron	chemical	The background oxidation of iron at 20 and 100 μM in enzyme-free controls are shown for reference. (B) Encapsulin and EncFtn-Enc complexes at 10 μM asymmetric unit concentration were incubated with Fe2+ at 20 and 100 μM and progress curves for iron oxidation at A315 were measured in a UV/visible spectrophotometer.	FIG
+286	314	UV/visible spectrophotometer	experimental_method	The background oxidation of iron at 20 and 100 μM in enzyme-free controls are shown for reference. (B) Encapsulin and EncFtn-Enc complexes at 10 μM asymmetric unit concentration were incubated with Fe2+ at 20 and 100 μM and progress curves for iron oxidation at A315 were measured in a UV/visible spectrophotometer.	FIG
+49	53	Fe2+	chemical	Enzyme free controls for background oxidation of Fe2+ are shown for reference. (C) Histogram of the iron loading capacity per biological assembly of EncFtnsH, encapsulin, EncFtn-Enc and apoferritin.	FIG
+100	104	iron	chemical	Enzyme free controls for background oxidation of Fe2+ are shown for reference. (C) Histogram of the iron loading capacity per biological assembly of EncFtnsH, encapsulin, EncFtn-Enc and apoferritin.	FIG
+149	157	EncFtnsH	protein	Enzyme free controls for background oxidation of Fe2+ are shown for reference. (C) Histogram of the iron loading capacity per biological assembly of EncFtnsH, encapsulin, EncFtn-Enc and apoferritin.	FIG
+159	169	encapsulin	protein	Enzyme free controls for background oxidation of Fe2+ are shown for reference. (C) Histogram of the iron loading capacity per biological assembly of EncFtnsH, encapsulin, EncFtn-Enc and apoferritin.	FIG
+171	181	EncFtn-Enc	complex_assembly	Enzyme free controls for background oxidation of Fe2+ are shown for reference. (C) Histogram of the iron loading capacity per biological assembly of EncFtnsH, encapsulin, EncFtn-Enc and apoferritin.	FIG
+186	197	apoferritin	protein_state	Enzyme free controls for background oxidation of Fe2+ are shown for reference. (C) Histogram of the iron loading capacity per biological assembly of EncFtnsH, encapsulin, EncFtn-Enc and apoferritin.	FIG
+79	83	iron	chemical	The results shown are for three technical replicates and represent the optimal iron loading by the complexes after three hours when incubated with Fe2+.	FIG
+147	151	Fe2+	chemical	The results shown are for three technical replicates and represent the optimal iron loading by the complexes after three hours when incubated with Fe2+.	FIG
+37	48	iron-loaded	protein_state	In light of the identification of an iron-loaded FOC in the crystal structure of EncFtn and our native mass spectrometry data, we performed ferroxidase and peroxidase assays to demonstrate the catalytic activity of this protein.	RESULTS
+49	52	FOC	site	In light of the identification of an iron-loaded FOC in the crystal structure of EncFtn and our native mass spectrometry data, we performed ferroxidase and peroxidase assays to demonstrate the catalytic activity of this protein.	RESULTS
+60	77	crystal structure	evidence	In light of the identification of an iron-loaded FOC in the crystal structure of EncFtn and our native mass spectrometry data, we performed ferroxidase and peroxidase assays to demonstrate the catalytic activity of this protein.	RESULTS
+81	87	EncFtn	protein	In light of the identification of an iron-loaded FOC in the crystal structure of EncFtn and our native mass spectrometry data, we performed ferroxidase and peroxidase assays to demonstrate the catalytic activity of this protein.	RESULTS
+96	120	native mass spectrometry	experimental_method	In light of the identification of an iron-loaded FOC in the crystal structure of EncFtn and our native mass spectrometry data, we performed ferroxidase and peroxidase assays to demonstrate the catalytic activity of this protein.	RESULTS
+140	173	ferroxidase and peroxidase assays	experimental_method	In light of the identification of an iron-loaded FOC in the crystal structure of EncFtn and our native mass spectrometry data, we performed ferroxidase and peroxidase assays to demonstrate the catalytic activity of this protein.	RESULTS
+29	35	equine	taxonomy_domain	In addition, we also assayed equine apoferritin, an example of a classical ferritin enzyme, as a positive control.	RESULTS
+36	47	apoferritin	protein_state	In addition, we also assayed equine apoferritin, an example of a classical ferritin enzyme, as a positive control.	RESULTS
+65	74	classical	protein_state	In addition, we also assayed equine apoferritin, an example of a classical ferritin enzyme, as a positive control.	RESULTS
+75	83	ferritin	protein_type	In addition, we also assayed equine apoferritin, an example of a classical ferritin enzyme, as a positive control.	RESULTS
+11	21	Dps family	protein_type	Unlike the Dps family of ferritin-like proteins, EncFtn showed no peroxidase activity when assayed with the substrate ortho-phenylenediamine.	RESULTS
+25	47	ferritin-like proteins	protein_type	Unlike the Dps family of ferritin-like proteins, EncFtn showed no peroxidase activity when assayed with the substrate ortho-phenylenediamine.	RESULTS
+49	55	EncFtn	protein	Unlike the Dps family of ferritin-like proteins, EncFtn showed no peroxidase activity when assayed with the substrate ortho-phenylenediamine.	RESULTS
+118	140	ortho-phenylenediamine	chemical	Unlike the Dps family of ferritin-like proteins, EncFtn showed no peroxidase activity when assayed with the substrate ortho-phenylenediamine.	RESULTS
+4	15	ferroxidase	protein_type	The ferroxidase activity of EncFtnsH was measured by recording the progress curve of Fe2+ oxidation to Fe3+ at 315 nm after addition of 20 and 100 µM Fe2+ (2 and 10 times molar ratio Fe2+/FOC).	RESULTS
+28	36	EncFtnsH	protein	The ferroxidase activity of EncFtnsH was measured by recording the progress curve of Fe2+ oxidation to Fe3+ at 315 nm after addition of 20 and 100 µM Fe2+ (2 and 10 times molar ratio Fe2+/FOC).	RESULTS
+67	81	progress curve	evidence	The ferroxidase activity of EncFtnsH was measured by recording the progress curve of Fe2+ oxidation to Fe3+ at 315 nm after addition of 20 and 100 µM Fe2+ (2 and 10 times molar ratio Fe2+/FOC).	RESULTS
+85	89	Fe2+	chemical	The ferroxidase activity of EncFtnsH was measured by recording the progress curve of Fe2+ oxidation to Fe3+ at 315 nm after addition of 20 and 100 µM Fe2+ (2 and 10 times molar ratio Fe2+/FOC).	RESULTS
+103	107	Fe3+	chemical	The ferroxidase activity of EncFtnsH was measured by recording the progress curve of Fe2+ oxidation to Fe3+ at 315 nm after addition of 20 and 100 µM Fe2+ (2 and 10 times molar ratio Fe2+/FOC).	RESULTS
+150	154	Fe2+	chemical	The ferroxidase activity of EncFtnsH was measured by recording the progress curve of Fe2+ oxidation to Fe3+ at 315 nm after addition of 20 and 100 µM Fe2+ (2 and 10 times molar ratio Fe2+/FOC).	RESULTS
+183	187	Fe2+	chemical	The ferroxidase activity of EncFtnsH was measured by recording the progress curve of Fe2+ oxidation to Fe3+ at 315 nm after addition of 20 and 100 µM Fe2+ (2 and 10 times molar ratio Fe2+/FOC).	RESULTS
+188	191	FOC	site	The ferroxidase activity of EncFtnsH was measured by recording the progress curve of Fe2+ oxidation to Fe3+ at 315 nm after addition of 20 and 100 µM Fe2+ (2 and 10 times molar ratio Fe2+/FOC).	RESULTS
+82	86	Fe2+	chemical	In both experiments the rate of oxidation was faster than background oxidation of Fe2+ by molecular oxygen, and was highest for 100 µM Fe2+ (Figure 8A).	RESULTS
+100	106	oxygen	chemical	In both experiments the rate of oxidation was faster than background oxidation of Fe2+ by molecular oxygen, and was highest for 100 µM Fe2+ (Figure 8A).	RESULTS
+135	139	Fe2+	chemical	In both experiments the rate of oxidation was faster than background oxidation of Fe2+ by molecular oxygen, and was highest for 100 µM Fe2+ (Figure 8A).	RESULTS
+33	41	EncFtnsH	protein	These data show that recombinant EncFtnsH acts as an active ferroxidase enzyme.	RESULTS
+53	59	active	protein_state	These data show that recombinant EncFtnsH acts as an active ferroxidase enzyme.	RESULTS
+60	71	ferroxidase	protein_type	These data show that recombinant EncFtnsH acts as an active ferroxidase enzyme.	RESULTS
+17	28	apoferritin	protein_state	When compared to apoferritin, EncFtnsH oxidized Fe2+ at a slower rate and the reaction did not run to completion over the 1800 s of the experiment.	RESULTS
+30	38	EncFtnsH	protein	When compared to apoferritin, EncFtnsH oxidized Fe2+ at a slower rate and the reaction did not run to completion over the 1800 s of the experiment.	RESULTS
+48	52	Fe2+	chemical	When compared to apoferritin, EncFtnsH oxidized Fe2+ at a slower rate and the reaction did not run to completion over the 1800 s of the experiment.	RESULTS
+33	37	iron	chemical	Addition of higher quantities of iron resulted in the formation of a yellow/red precipitate at the end of the reaction.	RESULTS
+55	65	encapsulin	protein	We also performed these assays on purified recombinant encapsulin; which, when assayed alone, did not display ferroxidase activity above background Fe2+ oxidation (Figure 8B).	RESULTS
+110	121	ferroxidase	protein_type	We also performed these assays on purified recombinant encapsulin; which, when assayed alone, did not display ferroxidase activity above background Fe2+ oxidation (Figure 8B).	RESULTS
+148	152	Fe2+	chemical	We also performed these assays on purified recombinant encapsulin; which, when assayed alone, did not display ferroxidase activity above background Fe2+ oxidation (Figure 8B).	RESULTS
+30	34	full	protein_state	In contrast, complexes of the full EncFtn encapsulin nanocompartment (i.e. the EncFtn-Enc protein complex) displayed ferroxidase activity comparable to apoferritin without the formation of precipitates (Figure 8B).	RESULTS
+35	41	EncFtn	protein	In contrast, complexes of the full EncFtn encapsulin nanocompartment (i.e. the EncFtn-Enc protein complex) displayed ferroxidase activity comparable to apoferritin without the formation of precipitates (Figure 8B).	RESULTS
+42	52	encapsulin	protein	In contrast, complexes of the full EncFtn encapsulin nanocompartment (i.e. the EncFtn-Enc protein complex) displayed ferroxidase activity comparable to apoferritin without the formation of precipitates (Figure 8B).	RESULTS
+53	68	nanocompartment	complex_assembly	In contrast, complexes of the full EncFtn encapsulin nanocompartment (i.e. the EncFtn-Enc protein complex) displayed ferroxidase activity comparable to apoferritin without the formation of precipitates (Figure 8B).	RESULTS
+79	89	EncFtn-Enc	complex_assembly	In contrast, complexes of the full EncFtn encapsulin nanocompartment (i.e. the EncFtn-Enc protein complex) displayed ferroxidase activity comparable to apoferritin without the formation of precipitates (Figure 8B).	RESULTS
+117	128	ferroxidase	protein_type	In contrast, complexes of the full EncFtn encapsulin nanocompartment (i.e. the EncFtn-Enc protein complex) displayed ferroxidase activity comparable to apoferritin without the formation of precipitates (Figure 8B).	RESULTS
+152	163	apoferritin	protein_state	In contrast, complexes of the full EncFtn encapsulin nanocompartment (i.e. the EncFtn-Enc protein complex) displayed ferroxidase activity comparable to apoferritin without the formation of precipitates (Figure 8B).	RESULTS
+47	55	EncFtnsH	protein	We attributed the precipitates observed in the EncFtnsH ferroxidase assay to the production of insoluble Fe3+ complexes, which led us to propose that EncFtn does not directly store Fe3+ in a mineral form.	RESULTS
+56	73	ferroxidase assay	experimental_method	We attributed the precipitates observed in the EncFtnsH ferroxidase assay to the production of insoluble Fe3+ complexes, which led us to propose that EncFtn does not directly store Fe3+ in a mineral form.	RESULTS
+105	109	Fe3+	chemical	We attributed the precipitates observed in the EncFtnsH ferroxidase assay to the production of insoluble Fe3+ complexes, which led us to propose that EncFtn does not directly store Fe3+ in a mineral form.	RESULTS
+150	156	EncFtn	protein	We attributed the precipitates observed in the EncFtnsH ferroxidase assay to the production of insoluble Fe3+ complexes, which led us to propose that EncFtn does not directly store Fe3+ in a mineral form.	RESULTS
+181	185	Fe3+	chemical	We attributed the precipitates observed in the EncFtnsH ferroxidase assay to the production of insoluble Fe3+ complexes, which led us to propose that EncFtn does not directly store Fe3+ in a mineral form.	RESULTS
+29	38	native MS	experimental_method	This observation agrees with native MS results, which indicates a maximum iron loading of 10–15 iron ions per decameric EncFtn; and the structure, which does not possess the enclosed iron-storage cavity characteristic of classical ferritins and Dps family proteins that can directly accrue mineralized Fe3+ within their nanocompartment structures.	RESULTS
+74	78	iron	chemical	This observation agrees with native MS results, which indicates a maximum iron loading of 10–15 iron ions per decameric EncFtn; and the structure, which does not possess the enclosed iron-storage cavity characteristic of classical ferritins and Dps family proteins that can directly accrue mineralized Fe3+ within their nanocompartment structures.	RESULTS
+96	100	iron	chemical	This observation agrees with native MS results, which indicates a maximum iron loading of 10–15 iron ions per decameric EncFtn; and the structure, which does not possess the enclosed iron-storage cavity characteristic of classical ferritins and Dps family proteins that can directly accrue mineralized Fe3+ within their nanocompartment structures.	RESULTS
+110	119	decameric	oligomeric_state	This observation agrees with native MS results, which indicates a maximum iron loading of 10–15 iron ions per decameric EncFtn; and the structure, which does not possess the enclosed iron-storage cavity characteristic of classical ferritins and Dps family proteins that can directly accrue mineralized Fe3+ within their nanocompartment structures.	RESULTS
+120	126	EncFtn	protein	This observation agrees with native MS results, which indicates a maximum iron loading of 10–15 iron ions per decameric EncFtn; and the structure, which does not possess the enclosed iron-storage cavity characteristic of classical ferritins and Dps family proteins that can directly accrue mineralized Fe3+ within their nanocompartment structures.	RESULTS
+136	145	structure	evidence	This observation agrees with native MS results, which indicates a maximum iron loading of 10–15 iron ions per decameric EncFtn; and the structure, which does not possess the enclosed iron-storage cavity characteristic of classical ferritins and Dps family proteins that can directly accrue mineralized Fe3+ within their nanocompartment structures.	RESULTS
+183	202	iron-storage cavity	site	This observation agrees with native MS results, which indicates a maximum iron loading of 10–15 iron ions per decameric EncFtn; and the structure, which does not possess the enclosed iron-storage cavity characteristic of classical ferritins and Dps family proteins that can directly accrue mineralized Fe3+ within their nanocompartment structures.	RESULTS
+221	230	classical	protein_state	This observation agrees with native MS results, which indicates a maximum iron loading of 10–15 iron ions per decameric EncFtn; and the structure, which does not possess the enclosed iron-storage cavity characteristic of classical ferritins and Dps family proteins that can directly accrue mineralized Fe3+ within their nanocompartment structures.	RESULTS
+231	240	ferritins	protein_type	This observation agrees with native MS results, which indicates a maximum iron loading of 10–15 iron ions per decameric EncFtn; and the structure, which does not possess the enclosed iron-storage cavity characteristic of classical ferritins and Dps family proteins that can directly accrue mineralized Fe3+ within their nanocompartment structures.	RESULTS
+245	264	Dps family proteins	protein_type	This observation agrees with native MS results, which indicates a maximum iron loading of 10–15 iron ions per decameric EncFtn; and the structure, which does not possess the enclosed iron-storage cavity characteristic of classical ferritins and Dps family proteins that can directly accrue mineralized Fe3+ within their nanocompartment structures.	RESULTS
+302	306	Fe3+	chemical	This observation agrees with native MS results, which indicates a maximum iron loading of 10–15 iron ions per decameric EncFtn; and the structure, which does not possess the enclosed iron-storage cavity characteristic of classical ferritins and Dps family proteins that can directly accrue mineralized Fe3+ within their nanocompartment structures.	RESULTS
+320	335	nanocompartment	complex_assembly	This observation agrees with native MS results, which indicates a maximum iron loading of 10–15 iron ions per decameric EncFtn; and the structure, which does not possess the enclosed iron-storage cavity characteristic of classical ferritins and Dps family proteins that can directly accrue mineralized Fe3+ within their nanocompartment structures.	RESULTS
+336	346	structures	evidence	This observation agrees with native MS results, which indicates a maximum iron loading of 10–15 iron ions per decameric EncFtn; and the structure, which does not possess the enclosed iron-storage cavity characteristic of classical ferritins and Dps family proteins that can directly accrue mineralized Fe3+ within their nanocompartment structures.	RESULTS
+69	75	EncFtn	protein	To analyze the products of these reactions and determine whether the EncFtn and encapsulin were able to store iron in a mineral form, we performed TEM on the reaction mixtures from the ferroxidase assay.	RESULTS
+80	90	encapsulin	protein	To analyze the products of these reactions and determine whether the EncFtn and encapsulin were able to store iron in a mineral form, we performed TEM on the reaction mixtures from the ferroxidase assay.	RESULTS
+110	114	iron	chemical	To analyze the products of these reactions and determine whether the EncFtn and encapsulin were able to store iron in a mineral form, we performed TEM on the reaction mixtures from the ferroxidase assay.	RESULTS
+147	150	TEM	experimental_method	To analyze the products of these reactions and determine whether the EncFtn and encapsulin were able to store iron in a mineral form, we performed TEM on the reaction mixtures from the ferroxidase assay.	RESULTS
+185	202	ferroxidase assay	experimental_method	To analyze the products of these reactions and determine whether the EncFtn and encapsulin were able to store iron in a mineral form, we performed TEM on the reaction mixtures from the ferroxidase assay.	RESULTS
+4	12	EncFtnsH	protein	The EncFtnsH reaction mixture showed the formation of large, irregular electron-dense precipitates (Figure 8—figure supplement 1A).	RESULTS
+67	71	Fe2+	chemical	A similar distribution of particles was observed after addition of Fe2+ to the encapsulin protein (Figure 8—figure supplement 1B).	RESULTS
+79	89	encapsulin	protein	A similar distribution of particles was observed after addition of Fe2+ to the encapsulin protein (Figure 8—figure supplement 1B).	RESULTS
+25	29	Fe2+	chemical	In contrast, addition of Fe2+ to the EncFtn-Enc nanocompartment resulted in small, highly regular, electron dense particles of approximately 5 nm in diameter (Figure 8—figure supplement 1C); we interpret these observations as controlled mineralization of iron within the nanocompartment.	RESULTS
+37	47	EncFtn-Enc	complex_assembly	In contrast, addition of Fe2+ to the EncFtn-Enc nanocompartment resulted in small, highly regular, electron dense particles of approximately 5 nm in diameter (Figure 8—figure supplement 1C); we interpret these observations as controlled mineralization of iron within the nanocompartment.	RESULTS
+48	63	nanocompartment	complex_assembly	In contrast, addition of Fe2+ to the EncFtn-Enc nanocompartment resulted in small, highly regular, electron dense particles of approximately 5 nm in diameter (Figure 8—figure supplement 1C); we interpret these observations as controlled mineralization of iron within the nanocompartment.	RESULTS
+255	259	iron	chemical	In contrast, addition of Fe2+ to the EncFtn-Enc nanocompartment resulted in small, highly regular, electron dense particles of approximately 5 nm in diameter (Figure 8—figure supplement 1C); we interpret these observations as controlled mineralization of iron within the nanocompartment.	RESULTS
+271	286	nanocompartment	complex_assembly	In contrast, addition of Fe2+ to the EncFtn-Enc nanocompartment resulted in small, highly regular, electron dense particles of approximately 5 nm in diameter (Figure 8—figure supplement 1C); we interpret these observations as controlled mineralization of iron within the nanocompartment.	RESULTS
+12	16	Fe2+	chemical	Addition of Fe2+ to apoferritin resulted in a mixture of large particles and small (~2 nm) particles consistent with partial mineralization by the ferritin and some background oxidation of the iron (Figure 8—figure supplement 1D).	RESULTS
+20	31	apoferritin	protein_state	Addition of Fe2+ to apoferritin resulted in a mixture of large particles and small (~2 nm) particles consistent with partial mineralization by the ferritin and some background oxidation of the iron (Figure 8—figure supplement 1D).	RESULTS
+147	155	ferritin	protein_type	Addition of Fe2+ to apoferritin resulted in a mixture of large particles and small (~2 nm) particles consistent with partial mineralization by the ferritin and some background oxidation of the iron (Figure 8—figure supplement 1D).	RESULTS
+193	197	iron	chemical	Addition of Fe2+ to apoferritin resulted in a mixture of large particles and small (~2 nm) particles consistent with partial mineralization by the ferritin and some background oxidation of the iron (Figure 8—figure supplement 1D).	RESULTS
+0	18	Negative stain TEM	experimental_method	Negative stain TEM of these samples revealed that upon addition of iron, the EncFtnsH protein showed significant aggregation (Figure 8—figure supplement 1F); while the encapsulin, EncFtn-Enc system, and apoferritin are present as distinct nanocompartments without significant protein aggregation (Figure 8—figure supplement 1G–I).	RESULTS
+67	71	iron	chemical	Negative stain TEM of these samples revealed that upon addition of iron, the EncFtnsH protein showed significant aggregation (Figure 8—figure supplement 1F); while the encapsulin, EncFtn-Enc system, and apoferritin are present as distinct nanocompartments without significant protein aggregation (Figure 8—figure supplement 1G–I).	RESULTS
+77	85	EncFtnsH	protein	Negative stain TEM of these samples revealed that upon addition of iron, the EncFtnsH protein showed significant aggregation (Figure 8—figure supplement 1F); while the encapsulin, EncFtn-Enc system, and apoferritin are present as distinct nanocompartments without significant protein aggregation (Figure 8—figure supplement 1G–I).	RESULTS
+168	178	encapsulin	protein	Negative stain TEM of these samples revealed that upon addition of iron, the EncFtnsH protein showed significant aggregation (Figure 8—figure supplement 1F); while the encapsulin, EncFtn-Enc system, and apoferritin are present as distinct nanocompartments without significant protein aggregation (Figure 8—figure supplement 1G–I).	RESULTS
+180	190	EncFtn-Enc	complex_assembly	Negative stain TEM of these samples revealed that upon addition of iron, the EncFtnsH protein showed significant aggregation (Figure 8—figure supplement 1F); while the encapsulin, EncFtn-Enc system, and apoferritin are present as distinct nanocompartments without significant protein aggregation (Figure 8—figure supplement 1G–I).	RESULTS
+203	214	apoferritin	protein_state	Negative stain TEM of these samples revealed that upon addition of iron, the EncFtnsH protein showed significant aggregation (Figure 8—figure supplement 1F); while the encapsulin, EncFtn-Enc system, and apoferritin are present as distinct nanocompartments without significant protein aggregation (Figure 8—figure supplement 1G–I).	RESULTS
+239	255	nanocompartments	complex_assembly	Negative stain TEM of these samples revealed that upon addition of iron, the EncFtnsH protein showed significant aggregation (Figure 8—figure supplement 1F); while the encapsulin, EncFtn-Enc system, and apoferritin are present as distinct nanocompartments without significant protein aggregation (Figure 8—figure supplement 1G–I).	RESULTS
+0	4	Iron	chemical	Iron storage in encapsulin nanocompartments	RESULTS
+16	26	encapsulin	protein	Iron storage in encapsulin nanocompartments	RESULTS
+27	43	nanocompartments	complex_assembly	Iron storage in encapsulin nanocompartments	RESULTS
+19	36	ferroxidase assay	experimental_method	The results of the ferroxidase assay and micrographs of the reaction products suggest that the oxidation and mineralization function of the classical ferritins are split between the EncFtn and encapsulin proteins, with the EncFtn acting as a ferroxidase and the encapsulin shell providing an environment and template for iron mineralization and storage.	RESULTS
+41	52	micrographs	evidence	The results of the ferroxidase assay and micrographs of the reaction products suggest that the oxidation and mineralization function of the classical ferritins are split between the EncFtn and encapsulin proteins, with the EncFtn acting as a ferroxidase and the encapsulin shell providing an environment and template for iron mineralization and storage.	RESULTS
+140	149	classical	protein_state	The results of the ferroxidase assay and micrographs of the reaction products suggest that the oxidation and mineralization function of the classical ferritins are split between the EncFtn and encapsulin proteins, with the EncFtn acting as a ferroxidase and the encapsulin shell providing an environment and template for iron mineralization and storage.	RESULTS
+150	159	ferritins	protein_type	The results of the ferroxidase assay and micrographs of the reaction products suggest that the oxidation and mineralization function of the classical ferritins are split between the EncFtn and encapsulin proteins, with the EncFtn acting as a ferroxidase and the encapsulin shell providing an environment and template for iron mineralization and storage.	RESULTS
+182	188	EncFtn	protein	The results of the ferroxidase assay and micrographs of the reaction products suggest that the oxidation and mineralization function of the classical ferritins are split between the EncFtn and encapsulin proteins, with the EncFtn acting as a ferroxidase and the encapsulin shell providing an environment and template for iron mineralization and storage.	RESULTS
+193	203	encapsulin	protein	The results of the ferroxidase assay and micrographs of the reaction products suggest that the oxidation and mineralization function of the classical ferritins are split between the EncFtn and encapsulin proteins, with the EncFtn acting as a ferroxidase and the encapsulin shell providing an environment and template for iron mineralization and storage.	RESULTS
+223	229	EncFtn	protein	The results of the ferroxidase assay and micrographs of the reaction products suggest that the oxidation and mineralization function of the classical ferritins are split between the EncFtn and encapsulin proteins, with the EncFtn acting as a ferroxidase and the encapsulin shell providing an environment and template for iron mineralization and storage.	RESULTS
+242	253	ferroxidase	protein_type	The results of the ferroxidase assay and micrographs of the reaction products suggest that the oxidation and mineralization function of the classical ferritins are split between the EncFtn and encapsulin proteins, with the EncFtn acting as a ferroxidase and the encapsulin shell providing an environment and template for iron mineralization and storage.	RESULTS
+262	272	encapsulin	protein	The results of the ferroxidase assay and micrographs of the reaction products suggest that the oxidation and mineralization function of the classical ferritins are split between the EncFtn and encapsulin proteins, with the EncFtn acting as a ferroxidase and the encapsulin shell providing an environment and template for iron mineralization and storage.	RESULTS
+273	278	shell	structure_element	The results of the ferroxidase assay and micrographs of the reaction products suggest that the oxidation and mineralization function of the classical ferritins are split between the EncFtn and encapsulin proteins, with the EncFtn acting as a ferroxidase and the encapsulin shell providing an environment and template for iron mineralization and storage.	RESULTS
+321	325	iron	chemical	The results of the ferroxidase assay and micrographs of the reaction products suggest that the oxidation and mineralization function of the classical ferritins are split between the EncFtn and encapsulin proteins, with the EncFtn acting as a ferroxidase and the encapsulin shell providing an environment and template for iron mineralization and storage.	RESULTS
+38	42	Fe2+	chemical	To investigate this further, we added Fe2+ at various concentrations to samples of apo-ferritin, EncFtn, isolated encapsulin, and the EncFtn-Enc protein complex, and subjected these samples to a ferrozine assay to quantify the amount of iron associated with the proteins after three hours of incubation.	RESULTS
+83	86	apo	protein_state	To investigate this further, we added Fe2+ at various concentrations to samples of apo-ferritin, EncFtn, isolated encapsulin, and the EncFtn-Enc protein complex, and subjected these samples to a ferrozine assay to quantify the amount of iron associated with the proteins after three hours of incubation.	RESULTS
+87	95	ferritin	protein_type	To investigate this further, we added Fe2+ at various concentrations to samples of apo-ferritin, EncFtn, isolated encapsulin, and the EncFtn-Enc protein complex, and subjected these samples to a ferrozine assay to quantify the amount of iron associated with the proteins after three hours of incubation.	RESULTS
+97	103	EncFtn	protein	To investigate this further, we added Fe2+ at various concentrations to samples of apo-ferritin, EncFtn, isolated encapsulin, and the EncFtn-Enc protein complex, and subjected these samples to a ferrozine assay to quantify the amount of iron associated with the proteins after three hours of incubation.	RESULTS
+114	124	encapsulin	protein	To investigate this further, we added Fe2+ at various concentrations to samples of apo-ferritin, EncFtn, isolated encapsulin, and the EncFtn-Enc protein complex, and subjected these samples to a ferrozine assay to quantify the amount of iron associated with the proteins after three hours of incubation.	RESULTS
+134	144	EncFtn-Enc	complex_assembly	To investigate this further, we added Fe2+ at various concentrations to samples of apo-ferritin, EncFtn, isolated encapsulin, and the EncFtn-Enc protein complex, and subjected these samples to a ferrozine assay to quantify the amount of iron associated with the proteins after three hours of incubation.	RESULTS
+195	210	ferrozine assay	experimental_method	To investigate this further, we added Fe2+ at various concentrations to samples of apo-ferritin, EncFtn, isolated encapsulin, and the EncFtn-Enc protein complex, and subjected these samples to a ferrozine assay to quantify the amount of iron associated with the proteins after three hours of incubation.	RESULTS
+237	241	iron	chemical	To investigate this further, we added Fe2+ at various concentrations to samples of apo-ferritin, EncFtn, isolated encapsulin, and the EncFtn-Enc protein complex, and subjected these samples to a ferrozine assay to quantify the amount of iron associated with the proteins after three hours of incubation.	RESULTS
+12	16	iron	chemical	The maximum iron loading capacity of these systems was calculated as the quantity of iron per biological assembly (Figure 8C).	RESULTS
+85	89	iron	chemical	The maximum iron loading capacity of these systems was calculated as the quantity of iron per biological assembly (Figure 8C).	RESULTS
+19	27	EncFtnsH	protein	In this assay, the EncFtnsH decamer binds a maximum of around 48 iron ions before excess iron induces protein precipitation.	RESULTS
+28	35	decamer	oligomeric_state	In this assay, the EncFtnsH decamer binds a maximum of around 48 iron ions before excess iron induces protein precipitation.	RESULTS
+65	69	iron	chemical	In this assay, the EncFtnsH decamer binds a maximum of around 48 iron ions before excess iron induces protein precipitation.	RESULTS
+89	93	iron	chemical	In this assay, the EncFtnsH decamer binds a maximum of around 48 iron ions before excess iron induces protein precipitation.	RESULTS
+4	14	encapsulin	protein	The encapsulin shell protein can sequester about 2200 iron ions before significant protein loss occurs, and the reconstituted EncFtn-Enc nanocompartment sequestered about 4150 iron ions.	RESULTS
+15	20	shell	structure_element	The encapsulin shell protein can sequester about 2200 iron ions before significant protein loss occurs, and the reconstituted EncFtn-Enc nanocompartment sequestered about 4150 iron ions.	RESULTS
+54	58	iron	chemical	The encapsulin shell protein can sequester about 2200 iron ions before significant protein loss occurs, and the reconstituted EncFtn-Enc nanocompartment sequestered about 4150 iron ions.	RESULTS
+126	136	EncFtn-Enc	complex_assembly	The encapsulin shell protein can sequester about 2200 iron ions before significant protein loss occurs, and the reconstituted EncFtn-Enc nanocompartment sequestered about 4150 iron ions.	RESULTS
+137	152	nanocompartment	complex_assembly	The encapsulin shell protein can sequester about 2200 iron ions before significant protein loss occurs, and the reconstituted EncFtn-Enc nanocompartment sequestered about 4150 iron ions.	RESULTS
+176	180	iron	chemical	The encapsulin shell protein can sequester about 2200 iron ions before significant protein loss occurs, and the reconstituted EncFtn-Enc nanocompartment sequestered about 4150 iron ions.	RESULTS
+50	61	apoferritin	protein_state	This latter result is significantly more than the apoferritin used in our assay, which sequesters approximately 570 iron ions in this assay (Figure 8C, Table 5).	RESULTS
+116	120	iron	chemical	This latter result is significantly more than the apoferritin used in our assay, which sequesters approximately 570 iron ions in this assay (Figure 8C, Table 5).	RESULTS
+75	81	EncFtn	protein	Consideration of the functional oligomeric states of these proteins, where EncFtn is a decamer and encapsulin forms an icosahedral cage, and estimation of the iron loading capacity of these complexes gives insight into the role of the two proteins in iron storage and mineralization.	RESULTS
+87	94	decamer	oligomeric_state	Consideration of the functional oligomeric states of these proteins, where EncFtn is a decamer and encapsulin forms an icosahedral cage, and estimation of the iron loading capacity of these complexes gives insight into the role of the two proteins in iron storage and mineralization.	RESULTS
+99	109	encapsulin	protein	Consideration of the functional oligomeric states of these proteins, where EncFtn is a decamer and encapsulin forms an icosahedral cage, and estimation of the iron loading capacity of these complexes gives insight into the role of the two proteins in iron storage and mineralization.	RESULTS
+119	130	icosahedral	protein_state	Consideration of the functional oligomeric states of these proteins, where EncFtn is a decamer and encapsulin forms an icosahedral cage, and estimation of the iron loading capacity of these complexes gives insight into the role of the two proteins in iron storage and mineralization.	RESULTS
+131	135	cage	complex_assembly	Consideration of the functional oligomeric states of these proteins, where EncFtn is a decamer and encapsulin forms an icosahedral cage, and estimation of the iron loading capacity of these complexes gives insight into the role of the two proteins in iron storage and mineralization.	RESULTS
+159	163	iron	chemical	Consideration of the functional oligomeric states of these proteins, where EncFtn is a decamer and encapsulin forms an icosahedral cage, and estimation of the iron loading capacity of these complexes gives insight into the role of the two proteins in iron storage and mineralization.	RESULTS
+251	255	iron	chemical	Consideration of the functional oligomeric states of these proteins, where EncFtn is a decamer and encapsulin forms an icosahedral cage, and estimation of the iron loading capacity of these complexes gives insight into the role of the two proteins in iron storage and mineralization.	RESULTS
+0	6	EncFtn	protein	EncFtn decamers bind up to 48 iron ions (Figure 8C), which is significantly higher than the stoichiometry of fifteen metal ions visible in the FOC and E31/34-site of the crystal structure of the EncFtnsH decamer and our MS analysis.	RESULTS
+7	15	decamers	oligomeric_state	EncFtn decamers bind up to 48 iron ions (Figure 8C), which is significantly higher than the stoichiometry of fifteen metal ions visible in the FOC and E31/34-site of the crystal structure of the EncFtnsH decamer and our MS analysis.	RESULTS
+30	34	iron	chemical	EncFtn decamers bind up to 48 iron ions (Figure 8C), which is significantly higher than the stoichiometry of fifteen metal ions visible in the FOC and E31/34-site of the crystal structure of the EncFtnsH decamer and our MS analysis.	RESULTS
+143	146	FOC	site	EncFtn decamers bind up to 48 iron ions (Figure 8C), which is significantly higher than the stoichiometry of fifteen metal ions visible in the FOC and E31/34-site of the crystal structure of the EncFtnsH decamer and our MS analysis.	RESULTS
+151	162	E31/34-site	site	EncFtn decamers bind up to 48 iron ions (Figure 8C), which is significantly higher than the stoichiometry of fifteen metal ions visible in the FOC and E31/34-site of the crystal structure of the EncFtnsH decamer and our MS analysis.	RESULTS
+170	187	crystal structure	evidence	EncFtn decamers bind up to 48 iron ions (Figure 8C), which is significantly higher than the stoichiometry of fifteen metal ions visible in the FOC and E31/34-site of the crystal structure of the EncFtnsH decamer and our MS analysis.	RESULTS
+195	203	EncFtnsH	protein	EncFtn decamers bind up to 48 iron ions (Figure 8C), which is significantly higher than the stoichiometry of fifteen metal ions visible in the FOC and E31/34-site of the crystal structure of the EncFtnsH decamer and our MS analysis.	RESULTS
+204	211	decamer	oligomeric_state	EncFtn decamers bind up to 48 iron ions (Figure 8C), which is significantly higher than the stoichiometry of fifteen metal ions visible in the FOC and E31/34-site of the crystal structure of the EncFtnsH decamer and our MS analysis.	RESULTS
+220	222	MS	experimental_method	EncFtn decamers bind up to 48 iron ions (Figure 8C), which is significantly higher than the stoichiometry of fifteen metal ions visible in the FOC and E31/34-site of the crystal structure of the EncFtnsH decamer and our MS analysis.	RESULTS
+30	51	solution measurements	experimental_method	The discrepancy between these solution measurements and our MS analysis may indicate that there are additional metal-binding sites on the interior channel and exterior faces of the protein; this is consistent with our identification of a number of weak metal-binding sites at the surface of the protein in the crystal structure (Figure 5D).	RESULTS
+60	62	MS	experimental_method	The discrepancy between these solution measurements and our MS analysis may indicate that there are additional metal-binding sites on the interior channel and exterior faces of the protein; this is consistent with our identification of a number of weak metal-binding sites at the surface of the protein in the crystal structure (Figure 5D).	RESULTS
+111	130	metal-binding sites	site	The discrepancy between these solution measurements and our MS analysis may indicate that there are additional metal-binding sites on the interior channel and exterior faces of the protein; this is consistent with our identification of a number of weak metal-binding sites at the surface of the protein in the crystal structure (Figure 5D).	RESULTS
+147	154	channel	site	The discrepancy between these solution measurements and our MS analysis may indicate that there are additional metal-binding sites on the interior channel and exterior faces of the protein; this is consistent with our identification of a number of weak metal-binding sites at the surface of the protein in the crystal structure (Figure 5D).	RESULTS
+253	272	metal-binding sites	site	The discrepancy between these solution measurements and our MS analysis may indicate that there are additional metal-binding sites on the interior channel and exterior faces of the protein; this is consistent with our identification of a number of weak metal-binding sites at the surface of the protein in the crystal structure (Figure 5D).	RESULTS
+310	327	crystal structure	evidence	The discrepancy between these solution measurements and our MS analysis may indicate that there are additional metal-binding sites on the interior channel and exterior faces of the protein; this is consistent with our identification of a number of weak metal-binding sites at the surface of the protein in the crystal structure (Figure 5D).	RESULTS
+48	52	Fe2+	chemical	These observations are consistent with hydrated Fe2+ ions being channeled to the active site from the E31/34-site and the subsequent exit of Fe3+ products on the outer surface, as is seen in other ferritin family proteins.	RESULTS
+81	92	active site	site	These observations are consistent with hydrated Fe2+ ions being channeled to the active site from the E31/34-site and the subsequent exit of Fe3+ products on the outer surface, as is seen in other ferritin family proteins.	RESULTS
+102	113	E31/34-site	site	These observations are consistent with hydrated Fe2+ ions being channeled to the active site from the E31/34-site and the subsequent exit of Fe3+ products on the outer surface, as is seen in other ferritin family proteins.	RESULTS
+141	145	Fe3+	chemical	These observations are consistent with hydrated Fe2+ ions being channeled to the active site from the E31/34-site and the subsequent exit of Fe3+ products on the outer surface, as is seen in other ferritin family proteins.	RESULTS
+197	205	ferritin	protein_type	These observations are consistent with hydrated Fe2+ ions being channeled to the active site from the E31/34-site and the subsequent exit of Fe3+ products on the outer surface, as is seen in other ferritin family proteins.	RESULTS
+19	29	encapsulin	protein	While the isolated encapsulin shell does not display any ferroxidase activity, it binds around 2200 iron ions in our assay (Table 5).	RESULTS
+30	35	shell	structure_element	While the isolated encapsulin shell does not display any ferroxidase activity, it binds around 2200 iron ions in our assay (Table 5).	RESULTS
+57	68	ferroxidase	protein_type	While the isolated encapsulin shell does not display any ferroxidase activity, it binds around 2200 iron ions in our assay (Table 5).	RESULTS
+100	104	iron	chemical	While the isolated encapsulin shell does not display any ferroxidase activity, it binds around 2200 iron ions in our assay (Table 5).	RESULTS
+22	27	shell	structure_element	This implies that the shell can bind a significant amount of iron on its outer and inner surfaces.	RESULTS
+61	65	iron	chemical	This implies that the shell can bind a significant amount of iron on its outer and inner surfaces.	RESULTS
+47	56	classical	protein_state	While the maximum reported loading capacity of classical ferritins is approximately 4500 iron ions, in our assay system we were only able to load apoferritin with around 570 iron ions.	RESULTS
+57	66	ferritins	protein_type	While the maximum reported loading capacity of classical ferritins is approximately 4500 iron ions, in our assay system we were only able to load apoferritin with around 570 iron ions.	RESULTS
+89	93	iron	chemical	While the maximum reported loading capacity of classical ferritins is approximately 4500 iron ions, in our assay system we were only able to load apoferritin with around 570 iron ions.	RESULTS
+146	157	apoferritin	protein_state	While the maximum reported loading capacity of classical ferritins is approximately 4500 iron ions, in our assay system we were only able to load apoferritin with around 570 iron ions.	RESULTS
+174	178	iron	chemical	While the maximum reported loading capacity of classical ferritins is approximately 4500 iron ions, in our assay system we were only able to load apoferritin with around 570 iron ions.	RESULTS
+25	35	EncFtn-Enc	complex_assembly	However, the recombinant EncFtn-Enc nanocompartment was able to bind over 4100 iron ions in the same time period, over seven times the amount seen for the apoferritin.	RESULTS
+36	51	nanocompartment	complex_assembly	However, the recombinant EncFtn-Enc nanocompartment was able to bind over 4100 iron ions in the same time period, over seven times the amount seen for the apoferritin.	RESULTS
+79	83	iron	chemical	However, the recombinant EncFtn-Enc nanocompartment was able to bind over 4100 iron ions in the same time period, over seven times the amount seen for the apoferritin.	RESULTS
+155	166	apoferritin	protein_state	However, the recombinant EncFtn-Enc nanocompartment was able to bind over 4100 iron ions in the same time period, over seven times the amount seen for the apoferritin.	RESULTS
+49	53	iron	chemical	We note we do not reach the experimental maximum iron loading for apoferritin and therefore the total iron-loading capacity of our system may be significantly higher than in this experimental system.	RESULTS
+66	77	apoferritin	protein_state	We note we do not reach the experimental maximum iron loading for apoferritin and therefore the total iron-loading capacity of our system may be significantly higher than in this experimental system.	RESULTS
+102	106	iron	chemical	We note we do not reach the experimental maximum iron loading for apoferritin and therefore the total iron-loading capacity of our system may be significantly higher than in this experimental system.	RESULTS
+35	41	EncFtn	protein	Taken together, our data show that EncFtn can catalytically oxidize Fe2+ to Fe3+; however, iron binding in EncFtn is limited to the FOC and several surface metal binding sites.	RESULTS
+68	72	Fe2+	chemical	Taken together, our data show that EncFtn can catalytically oxidize Fe2+ to Fe3+; however, iron binding in EncFtn is limited to the FOC and several surface metal binding sites.	RESULTS
+76	80	Fe3+	chemical	Taken together, our data show that EncFtn can catalytically oxidize Fe2+ to Fe3+; however, iron binding in EncFtn is limited to the FOC and several surface metal binding sites.	RESULTS
+91	95	iron	chemical	Taken together, our data show that EncFtn can catalytically oxidize Fe2+ to Fe3+; however, iron binding in EncFtn is limited to the FOC and several surface metal binding sites.	RESULTS
+107	113	EncFtn	protein	Taken together, our data show that EncFtn can catalytically oxidize Fe2+ to Fe3+; however, iron binding in EncFtn is limited to the FOC and several surface metal binding sites.	RESULTS
+132	135	FOC	site	Taken together, our data show that EncFtn can catalytically oxidize Fe2+ to Fe3+; however, iron binding in EncFtn is limited to the FOC and several surface metal binding sites.	RESULTS
+156	175	metal binding sites	site	Taken together, our data show that EncFtn can catalytically oxidize Fe2+ to Fe3+; however, iron binding in EncFtn is limited to the FOC and several surface metal binding sites.	RESULTS
+17	27	encapsulin	protein	In contrast, the encapsulin protein displays no catalytic activity, but has the ability to bind a considerable amount of iron.	RESULTS
+121	125	iron	chemical	In contrast, the encapsulin protein displays no catalytic activity, but has the ability to bind a considerable amount of iron.	RESULTS
+13	23	EncFtn-Enc	complex_assembly	Finally, the EncFtn-Enc nanocompartment complex retains the catalytic activity of EncFtn, and sequesters iron within the encapsulin shell at a higher level than the isolated components of the system, and at a significantly higher level than the classical ferritins.	RESULTS
+24	39	nanocompartment	complex_assembly	Finally, the EncFtn-Enc nanocompartment complex retains the catalytic activity of EncFtn, and sequesters iron within the encapsulin shell at a higher level than the isolated components of the system, and at a significantly higher level than the classical ferritins.	RESULTS
+82	88	EncFtn	protein	Finally, the EncFtn-Enc nanocompartment complex retains the catalytic activity of EncFtn, and sequesters iron within the encapsulin shell at a higher level than the isolated components of the system, and at a significantly higher level than the classical ferritins.	RESULTS
+105	109	iron	chemical	Finally, the EncFtn-Enc nanocompartment complex retains the catalytic activity of EncFtn, and sequesters iron within the encapsulin shell at a higher level than the isolated components of the system, and at a significantly higher level than the classical ferritins.	RESULTS
+121	131	encapsulin	protein	Finally, the EncFtn-Enc nanocompartment complex retains the catalytic activity of EncFtn, and sequesters iron within the encapsulin shell at a higher level than the isolated components of the system, and at a significantly higher level than the classical ferritins.	RESULTS
+132	137	shell	structure_element	Finally, the EncFtn-Enc nanocompartment complex retains the catalytic activity of EncFtn, and sequesters iron within the encapsulin shell at a higher level than the isolated components of the system, and at a significantly higher level than the classical ferritins.	RESULTS
+245	254	classical	protein_state	Finally, the EncFtn-Enc nanocompartment complex retains the catalytic activity of EncFtn, and sequesters iron within the encapsulin shell at a higher level than the isolated components of the system, and at a significantly higher level than the classical ferritins.	RESULTS
+255	264	ferritins	protein_type	Finally, the EncFtn-Enc nanocompartment complex retains the catalytic activity of EncFtn, and sequesters iron within the encapsulin shell at a higher level than the isolated components of the system, and at a significantly higher level than the classical ferritins.	RESULTS
+30	46	nanocompartments	complex_assembly	 Furthermore, our recombinant nanocompartments may not have the physiological subunit stoichiometry, and the iron-loading capacity of native nanocompartments is potentially much higher than the level we have observed.	RESULTS
+109	113	iron	chemical	 Furthermore, our recombinant nanocompartments may not have the physiological subunit stoichiometry, and the iron-loading capacity of native nanocompartments is potentially much higher than the level we have observed.	RESULTS
+134	140	native	protein_state	 Furthermore, our recombinant nanocompartments may not have the physiological subunit stoichiometry, and the iron-loading capacity of native nanocompartments is potentially much higher than the level we have observed.	RESULTS
+141	157	nanocompartments	complex_assembly	 Furthermore, our recombinant nanocompartments may not have the physiological subunit stoichiometry, and the iron-loading capacity of native nanocompartments is potentially much higher than the level we have observed.	RESULTS
+0	11	Mutagenesis	experimental_method	Mutagenesis of the EncFtnsHferroxidase center	RESULTS
+19	27	EncFtnsH	protein	Mutagenesis of the EncFtnsHferroxidase center	RESULTS
+27	45	ferroxidase center	site	Mutagenesis of the EncFtnsHferroxidase center	RESULTS
+28	37	R. rubrum	species	Purification of recombinant R. rubrum EncFtnsH FOC mutants.	FIG
+38	46	EncFtnsH	protein	Purification of recombinant R. rubrum EncFtnsH FOC mutants.	FIG
+47	50	FOC	site	Purification of recombinant R. rubrum EncFtnsH FOC mutants.	FIG
+51	58	mutants	protein_state	Purification of recombinant R. rubrum EncFtnsH FOC mutants.	FIG
+7	14	mutants	protein_state	Single mutants E32A, E62A, and H65A of EncFtnsH produced from E. coli BL21(DE3) cells grown in MM and MM supplemented with iron were subjected to Superdex 200 size-exclusion chromatography.	FIG
+15	19	E32A	mutant	Single mutants E32A, E62A, and H65A of EncFtnsH produced from E. coli BL21(DE3) cells grown in MM and MM supplemented with iron were subjected to Superdex 200 size-exclusion chromatography.	FIG
+21	25	E62A	mutant	Single mutants E32A, E62A, and H65A of EncFtnsH produced from E. coli BL21(DE3) cells grown in MM and MM supplemented with iron were subjected to Superdex 200 size-exclusion chromatography.	FIG
+31	35	H65A	mutant	Single mutants E32A, E62A, and H65A of EncFtnsH produced from E. coli BL21(DE3) cells grown in MM and MM supplemented with iron were subjected to Superdex 200 size-exclusion chromatography.	FIG
+39	47	EncFtnsH	protein	Single mutants E32A, E62A, and H65A of EncFtnsH produced from E. coli BL21(DE3) cells grown in MM and MM supplemented with iron were subjected to Superdex 200 size-exclusion chromatography.	FIG
+62	79	E. coli BL21(DE3)	species	Single mutants E32A, E62A, and H65A of EncFtnsH produced from E. coli BL21(DE3) cells grown in MM and MM supplemented with iron were subjected to Superdex 200 size-exclusion chromatography.	FIG
+95	97	MM	experimental_method	Single mutants E32A, E62A, and H65A of EncFtnsH produced from E. coli BL21(DE3) cells grown in MM and MM supplemented with iron were subjected to Superdex 200 size-exclusion chromatography.	FIG
+102	104	MM	experimental_method	Single mutants E32A, E62A, and H65A of EncFtnsH produced from E. coli BL21(DE3) cells grown in MM and MM supplemented with iron were subjected to Superdex 200 size-exclusion chromatography.	FIG
+123	127	iron	chemical	Single mutants E32A, E62A, and H65A of EncFtnsH produced from E. coli BL21(DE3) cells grown in MM and MM supplemented with iron were subjected to Superdex 200 size-exclusion chromatography.	FIG
+159	188	size-exclusion chromatography	experimental_method	Single mutants E32A, E62A, and H65A of EncFtnsH produced from E. coli BL21(DE3) cells grown in MM and MM supplemented with iron were subjected to Superdex 200 size-exclusion chromatography.	FIG
+4	31	Gel-filtration chromatogram	evidence	(A) Gel-filtration chromatogram of the E32A mutant form of EncFtnsH resulted in an elution profile with a majority of the protein eluting as the decameric form of the protein and a small proportion of monomer. (B) Gel-filtration chromatograhy of the E62A mutant form of EncFtnsH resulted in an elution profile with a single major decameric peak. (C) Gel-filtration chromatography of the H65A mutant form of EncFtnsH resulted in a single peak corresponding to the protein monomer.	FIG
+39	43	E32A	mutant	(A) Gel-filtration chromatogram of the E32A mutant form of EncFtnsH resulted in an elution profile with a majority of the protein eluting as the decameric form of the protein and a small proportion of monomer. (B) Gel-filtration chromatograhy of the E62A mutant form of EncFtnsH resulted in an elution profile with a single major decameric peak. (C) Gel-filtration chromatography of the H65A mutant form of EncFtnsH resulted in a single peak corresponding to the protein monomer.	FIG
+44	50	mutant	protein_state	(A) Gel-filtration chromatogram of the E32A mutant form of EncFtnsH resulted in an elution profile with a majority of the protein eluting as the decameric form of the protein and a small proportion of monomer. (B) Gel-filtration chromatograhy of the E62A mutant form of EncFtnsH resulted in an elution profile with a single major decameric peak. (C) Gel-filtration chromatography of the H65A mutant form of EncFtnsH resulted in a single peak corresponding to the protein monomer.	FIG
+59	67	EncFtnsH	protein	(A) Gel-filtration chromatogram of the E32A mutant form of EncFtnsH resulted in an elution profile with a majority of the protein eluting as the decameric form of the protein and a small proportion of monomer. (B) Gel-filtration chromatograhy of the E62A mutant form of EncFtnsH resulted in an elution profile with a single major decameric peak. (C) Gel-filtration chromatography of the H65A mutant form of EncFtnsH resulted in a single peak corresponding to the protein monomer.	FIG
+83	98	elution profile	evidence	(A) Gel-filtration chromatogram of the E32A mutant form of EncFtnsH resulted in an elution profile with a majority of the protein eluting as the decameric form of the protein and a small proportion of monomer. (B) Gel-filtration chromatograhy of the E62A mutant form of EncFtnsH resulted in an elution profile with a single major decameric peak. (C) Gel-filtration chromatography of the H65A mutant form of EncFtnsH resulted in a single peak corresponding to the protein monomer.	FIG
+145	154	decameric	oligomeric_state	(A) Gel-filtration chromatogram of the E32A mutant form of EncFtnsH resulted in an elution profile with a majority of the protein eluting as the decameric form of the protein and a small proportion of monomer. (B) Gel-filtration chromatograhy of the E62A mutant form of EncFtnsH resulted in an elution profile with a single major decameric peak. (C) Gel-filtration chromatography of the H65A mutant form of EncFtnsH resulted in a single peak corresponding to the protein monomer.	FIG
+201	208	monomer	oligomeric_state	(A) Gel-filtration chromatogram of the E32A mutant form of EncFtnsH resulted in an elution profile with a majority of the protein eluting as the decameric form of the protein and a small proportion of monomer. (B) Gel-filtration chromatograhy of the E62A mutant form of EncFtnsH resulted in an elution profile with a single major decameric peak. (C) Gel-filtration chromatography of the H65A mutant form of EncFtnsH resulted in a single peak corresponding to the protein monomer.	FIG
+214	242	Gel-filtration chromatograhy	experimental_method	(A) Gel-filtration chromatogram of the E32A mutant form of EncFtnsH resulted in an elution profile with a majority of the protein eluting as the decameric form of the protein and a small proportion of monomer. (B) Gel-filtration chromatograhy of the E62A mutant form of EncFtnsH resulted in an elution profile with a single major decameric peak. (C) Gel-filtration chromatography of the H65A mutant form of EncFtnsH resulted in a single peak corresponding to the protein monomer.	FIG
+250	254	E62A	mutant	(A) Gel-filtration chromatogram of the E32A mutant form of EncFtnsH resulted in an elution profile with a majority of the protein eluting as the decameric form of the protein and a small proportion of monomer. (B) Gel-filtration chromatograhy of the E62A mutant form of EncFtnsH resulted in an elution profile with a single major decameric peak. (C) Gel-filtration chromatography of the H65A mutant form of EncFtnsH resulted in a single peak corresponding to the protein monomer.	FIG
+255	261	mutant	protein_state	(A) Gel-filtration chromatogram of the E32A mutant form of EncFtnsH resulted in an elution profile with a majority of the protein eluting as the decameric form of the protein and a small proportion of monomer. (B) Gel-filtration chromatograhy of the E62A mutant form of EncFtnsH resulted in an elution profile with a single major decameric peak. (C) Gel-filtration chromatography of the H65A mutant form of EncFtnsH resulted in a single peak corresponding to the protein monomer.	FIG
+270	278	EncFtnsH	protein	(A) Gel-filtration chromatogram of the E32A mutant form of EncFtnsH resulted in an elution profile with a majority of the protein eluting as the decameric form of the protein and a small proportion of monomer. (B) Gel-filtration chromatograhy of the E62A mutant form of EncFtnsH resulted in an elution profile with a single major decameric peak. (C) Gel-filtration chromatography of the H65A mutant form of EncFtnsH resulted in a single peak corresponding to the protein monomer.	FIG
+294	309	elution profile	evidence	(A) Gel-filtration chromatogram of the E32A mutant form of EncFtnsH resulted in an elution profile with a majority of the protein eluting as the decameric form of the protein and a small proportion of monomer. (B) Gel-filtration chromatograhy of the E62A mutant form of EncFtnsH resulted in an elution profile with a single major decameric peak. (C) Gel-filtration chromatography of the H65A mutant form of EncFtnsH resulted in a single peak corresponding to the protein monomer.	FIG
+330	339	decameric	oligomeric_state	(A) Gel-filtration chromatogram of the E32A mutant form of EncFtnsH resulted in an elution profile with a majority of the protein eluting as the decameric form of the protein and a small proportion of monomer. (B) Gel-filtration chromatograhy of the E62A mutant form of EncFtnsH resulted in an elution profile with a single major decameric peak. (C) Gel-filtration chromatography of the H65A mutant form of EncFtnsH resulted in a single peak corresponding to the protein monomer.	FIG
+350	379	Gel-filtration chromatography	experimental_method	(A) Gel-filtration chromatogram of the E32A mutant form of EncFtnsH resulted in an elution profile with a majority of the protein eluting as the decameric form of the protein and a small proportion of monomer. (B) Gel-filtration chromatograhy of the E62A mutant form of EncFtnsH resulted in an elution profile with a single major decameric peak. (C) Gel-filtration chromatography of the H65A mutant form of EncFtnsH resulted in a single peak corresponding to the protein monomer.	FIG
+387	391	H65A	mutant	(A) Gel-filtration chromatogram of the E32A mutant form of EncFtnsH resulted in an elution profile with a majority of the protein eluting as the decameric form of the protein and a small proportion of monomer. (B) Gel-filtration chromatograhy of the E62A mutant form of EncFtnsH resulted in an elution profile with a single major decameric peak. (C) Gel-filtration chromatography of the H65A mutant form of EncFtnsH resulted in a single peak corresponding to the protein monomer.	FIG
+392	398	mutant	protein_state	(A) Gel-filtration chromatogram of the E32A mutant form of EncFtnsH resulted in an elution profile with a majority of the protein eluting as the decameric form of the protein and a small proportion of monomer. (B) Gel-filtration chromatograhy of the E62A mutant form of EncFtnsH resulted in an elution profile with a single major decameric peak. (C) Gel-filtration chromatography of the H65A mutant form of EncFtnsH resulted in a single peak corresponding to the protein monomer.	FIG
+407	415	EncFtnsH	protein	(A) Gel-filtration chromatogram of the E32A mutant form of EncFtnsH resulted in an elution profile with a majority of the protein eluting as the decameric form of the protein and a small proportion of monomer. (B) Gel-filtration chromatograhy of the E62A mutant form of EncFtnsH resulted in an elution profile with a single major decameric peak. (C) Gel-filtration chromatography of the H65A mutant form of EncFtnsH resulted in a single peak corresponding to the protein monomer.	FIG
+471	478	monomer	oligomeric_state	(A) Gel-filtration chromatogram of the E32A mutant form of EncFtnsH resulted in an elution profile with a majority of the protein eluting as the decameric form of the protein and a small proportion of monomer. (B) Gel-filtration chromatograhy of the E62A mutant form of EncFtnsH resulted in an elution profile with a single major decameric peak. (C) Gel-filtration chromatography of the H65A mutant form of EncFtnsH resulted in a single peak corresponding to the protein monomer.	FIG
+65	87	metal binding residues	site	To investigate the structural and biochemical role played by the metal binding residues in the di-iron FOC of EncFtnsH we produced alanine mutations in each of these residues: Glu32, Glu62, and His65.	RESULTS
+95	106	di-iron FOC	site	To investigate the structural and biochemical role played by the metal binding residues in the di-iron FOC of EncFtnsH we produced alanine mutations in each of these residues: Glu32, Glu62, and His65.	RESULTS
+110	118	EncFtnsH	protein	To investigate the structural and biochemical role played by the metal binding residues in the di-iron FOC of EncFtnsH we produced alanine mutations in each of these residues: Glu32, Glu62, and His65.	RESULTS
+131	148	alanine mutations	experimental_method	To investigate the structural and biochemical role played by the metal binding residues in the di-iron FOC of EncFtnsH we produced alanine mutations in each of these residues: Glu32, Glu62, and His65.	RESULTS
+176	181	Glu32	residue_name_number	To investigate the structural and biochemical role played by the metal binding residues in the di-iron FOC of EncFtnsH we produced alanine mutations in each of these residues: Glu32, Glu62, and His65.	RESULTS
+183	188	Glu62	residue_name_number	To investigate the structural and biochemical role played by the metal binding residues in the di-iron FOC of EncFtnsH we produced alanine mutations in each of these residues: Glu32, Glu62, and His65.	RESULTS
+194	199	His65	residue_name_number	To investigate the structural and biochemical role played by the metal binding residues in the di-iron FOC of EncFtnsH we produced alanine mutations in each of these residues: Glu32, Glu62, and His65.	RESULTS
+6	14	EncFtnsH	protein	These EncFtnsH mutants were produced in E. coli cells grown in MM, both in the absence and presence of additional iron.	RESULTS
+15	22	mutants	protein_state	These EncFtnsH mutants were produced in E. coli cells grown in MM, both in the absence and presence of additional iron.	RESULTS
+40	47	E. coli	species	These EncFtnsH mutants were produced in E. coli cells grown in MM, both in the absence and presence of additional iron.	RESULTS
+63	65	MM	experimental_method	These EncFtnsH mutants were produced in E. coli cells grown in MM, both in the absence and presence of additional iron.	RESULTS
+79	86	absence	protein_state	These EncFtnsH mutants were produced in E. coli cells grown in MM, both in the absence and presence of additional iron.	RESULTS
+91	102	presence of	protein_state	These EncFtnsH mutants were produced in E. coli cells grown in MM, both in the absence and presence of additional iron.	RESULTS
+114	118	iron	chemical	These EncFtnsH mutants were produced in E. coli cells grown in MM, both in the absence and presence of additional iron.	RESULTS
+4	8	E32A	mutant	The E32A and E62A mutants eluted from SEC at a volume consistent with the decameric form of EncFtnsH, with a small proportion of monomer; the H65A mutant eluted at a volume consistent with the monomeric form of EncFtnsH (Figure 9).	RESULTS
+13	17	E62A	mutant	The E32A and E62A mutants eluted from SEC at a volume consistent with the decameric form of EncFtnsH, with a small proportion of monomer; the H65A mutant eluted at a volume consistent with the monomeric form of EncFtnsH (Figure 9).	RESULTS
+18	25	mutants	protein_state	The E32A and E62A mutants eluted from SEC at a volume consistent with the decameric form of EncFtnsH, with a small proportion of monomer; the H65A mutant eluted at a volume consistent with the monomeric form of EncFtnsH (Figure 9).	RESULTS
+38	41	SEC	experimental_method	The E32A and E62A mutants eluted from SEC at a volume consistent with the decameric form of EncFtnsH, with a small proportion of monomer; the H65A mutant eluted at a volume consistent with the monomeric form of EncFtnsH (Figure 9).	RESULTS
+74	83	decameric	oligomeric_state	The E32A and E62A mutants eluted from SEC at a volume consistent with the decameric form of EncFtnsH, with a small proportion of monomer; the H65A mutant eluted at a volume consistent with the monomeric form of EncFtnsH (Figure 9).	RESULTS
+92	100	EncFtnsH	protein	The E32A and E62A mutants eluted from SEC at a volume consistent with the decameric form of EncFtnsH, with a small proportion of monomer; the H65A mutant eluted at a volume consistent with the monomeric form of EncFtnsH (Figure 9).	RESULTS
+129	136	monomer	oligomeric_state	The E32A and E62A mutants eluted from SEC at a volume consistent with the decameric form of EncFtnsH, with a small proportion of monomer; the H65A mutant eluted at a volume consistent with the monomeric form of EncFtnsH (Figure 9).	RESULTS
+142	146	H65A	mutant	The E32A and E62A mutants eluted from SEC at a volume consistent with the decameric form of EncFtnsH, with a small proportion of monomer; the H65A mutant eluted at a volume consistent with the monomeric form of EncFtnsH (Figure 9).	RESULTS
+147	153	mutant	protein_state	The E32A and E62A mutants eluted from SEC at a volume consistent with the decameric form of EncFtnsH, with a small proportion of monomer; the H65A mutant eluted at a volume consistent with the monomeric form of EncFtnsH (Figure 9).	RESULTS
+193	202	monomeric	oligomeric_state	The E32A and E62A mutants eluted from SEC at a volume consistent with the decameric form of EncFtnsH, with a small proportion of monomer; the H65A mutant eluted at a volume consistent with the monomeric form of EncFtnsH (Figure 9).	RESULTS
+211	219	EncFtnsH	protein	The E32A and E62A mutants eluted from SEC at a volume consistent with the decameric form of EncFtnsH, with a small proportion of monomer; the H65A mutant eluted at a volume consistent with the monomeric form of EncFtnsH (Figure 9).	RESULTS
+15	22	mutants	protein_state	For all of the mutants studied, no change in oligomerization state was apparent upon addition of Fe2+ in vitro.	RESULTS
+97	101	Fe2+	chemical	For all of the mutants studied, no change in oligomerization state was apparent upon addition of Fe2+ in vitro.	RESULTS
+0	24	Native mass spectrometry	experimental_method	Native mass spectrometry of EncFtnsH mutants.	FIG
+28	36	EncFtnsH	protein	Native mass spectrometry of EncFtnsH mutants.	FIG
+37	44	mutants	protein_state	Native mass spectrometry of EncFtnsH mutants.	FIG
+4	11	spectra	evidence	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Wild-type EncFtnsH in the absence of iron displays a charge state distribution consistent with a monomer (see also Figure 8). (B) E32A EncFtnsH displays a charge states consistent with a decamer (green circles); a minor species, consistent with the monomer of E32A mutant is also observed (blue circles).	FIG
+45	52	acetate	chemical	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Wild-type EncFtnsH in the absence of iron displays a charge state distribution consistent with a monomer (see also Figure 8). (B) E32A EncFtnsH displays a charge states consistent with a decamer (green circles); a minor species, consistent with the monomer of E32A mutant is also observed (blue circles).	FIG
+103	112	Wild-type	protein_state	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Wild-type EncFtnsH in the absence of iron displays a charge state distribution consistent with a monomer (see also Figure 8). (B) E32A EncFtnsH displays a charge states consistent with a decamer (green circles); a minor species, consistent with the monomer of E32A mutant is also observed (blue circles).	FIG
+113	121	EncFtnsH	protein	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Wild-type EncFtnsH in the absence of iron displays a charge state distribution consistent with a monomer (see also Figure 8). (B) E32A EncFtnsH displays a charge states consistent with a decamer (green circles); a minor species, consistent with the monomer of E32A mutant is also observed (blue circles).	FIG
+129	139	absence of	protein_state	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Wild-type EncFtnsH in the absence of iron displays a charge state distribution consistent with a monomer (see also Figure 8). (B) E32A EncFtnsH displays a charge states consistent with a decamer (green circles); a minor species, consistent with the monomer of E32A mutant is also observed (blue circles).	FIG
+140	144	iron	chemical	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Wild-type EncFtnsH in the absence of iron displays a charge state distribution consistent with a monomer (see also Figure 8). (B) E32A EncFtnsH displays a charge states consistent with a decamer (green circles); a minor species, consistent with the monomer of E32A mutant is also observed (blue circles).	FIG
+156	181	charge state distribution	evidence	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Wild-type EncFtnsH in the absence of iron displays a charge state distribution consistent with a monomer (see also Figure 8). (B) E32A EncFtnsH displays a charge states consistent with a decamer (green circles); a minor species, consistent with the monomer of E32A mutant is also observed (blue circles).	FIG
+200	207	monomer	oligomeric_state	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Wild-type EncFtnsH in the absence of iron displays a charge state distribution consistent with a monomer (see also Figure 8). (B) E32A EncFtnsH displays a charge states consistent with a decamer (green circles); a minor species, consistent with the monomer of E32A mutant is also observed (blue circles).	FIG
+233	237	E32A	mutant	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Wild-type EncFtnsH in the absence of iron displays a charge state distribution consistent with a monomer (see also Figure 8). (B) E32A EncFtnsH displays a charge states consistent with a decamer (green circles); a minor species, consistent with the monomer of E32A mutant is also observed (blue circles).	FIG
+238	246	EncFtnsH	protein	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Wild-type EncFtnsH in the absence of iron displays a charge state distribution consistent with a monomer (see also Figure 8). (B) E32A EncFtnsH displays a charge states consistent with a decamer (green circles); a minor species, consistent with the monomer of E32A mutant is also observed (blue circles).	FIG
+258	271	charge states	evidence	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Wild-type EncFtnsH in the absence of iron displays a charge state distribution consistent with a monomer (see also Figure 8). (B) E32A EncFtnsH displays a charge states consistent with a decamer (green circles); a minor species, consistent with the monomer of E32A mutant is also observed (blue circles).	FIG
+290	297	decamer	oligomeric_state	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Wild-type EncFtnsH in the absence of iron displays a charge state distribution consistent with a monomer (see also Figure 8). (B) E32A EncFtnsH displays a charge states consistent with a decamer (green circles); a minor species, consistent with the monomer of E32A mutant is also observed (blue circles).	FIG
+352	359	monomer	oligomeric_state	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Wild-type EncFtnsH in the absence of iron displays a charge state distribution consistent with a monomer (see also Figure 8). (B) E32A EncFtnsH displays a charge states consistent with a decamer (green circles); a minor species, consistent with the monomer of E32A mutant is also observed (blue circles).	FIG
+363	367	E32A	mutant	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Wild-type EncFtnsH in the absence of iron displays a charge state distribution consistent with a monomer (see also Figure 8). (B) E32A EncFtnsH displays a charge states consistent with a decamer (green circles); a minor species, consistent with the monomer of E32A mutant is also observed (blue circles).	FIG
+368	374	mutant	protein_state	All spectra were acquired in 100 mM ammonium acetate, pH 8.0 with a protein concentration of 5 µM. (A) Wild-type EncFtnsH in the absence of iron displays a charge state distribution consistent with a monomer (see also Figure 8). (B) E32A EncFtnsH displays a charge states consistent with a decamer (green circles); a minor species, consistent with the monomer of E32A mutant is also observed (blue circles).	FIG
+4	8	E62A	mutant	(C) E62A EncFtnsH displays charge states consistent with a decamer (green circles). (D) H65A EncFtnsH displays charge states consistent with both monomer (blue circles) and dimer (purple circles).	FIG
+9	17	EncFtnsH	protein	(C) E62A EncFtnsH displays charge states consistent with a decamer (green circles). (D) H65A EncFtnsH displays charge states consistent with both monomer (blue circles) and dimer (purple circles).	FIG
+27	40	charge states	evidence	(C) E62A EncFtnsH displays charge states consistent with a decamer (green circles). (D) H65A EncFtnsH displays charge states consistent with both monomer (blue circles) and dimer (purple circles).	FIG
+59	66	decamer	oligomeric_state	(C) E62A EncFtnsH displays charge states consistent with a decamer (green circles). (D) H65A EncFtnsH displays charge states consistent with both monomer (blue circles) and dimer (purple circles).	FIG
+88	92	H65A	mutant	(C) E62A EncFtnsH displays charge states consistent with a decamer (green circles). (D) H65A EncFtnsH displays charge states consistent with both monomer (blue circles) and dimer (purple circles).	FIG
+93	101	EncFtnsH	protein	(C) E62A EncFtnsH displays charge states consistent with a decamer (green circles). (D) H65A EncFtnsH displays charge states consistent with both monomer (blue circles) and dimer (purple circles).	FIG
+111	124	charge states	evidence	(C) E62A EncFtnsH displays charge states consistent with a decamer (green circles). (D) H65A EncFtnsH displays charge states consistent with both monomer (blue circles) and dimer (purple circles).	FIG
+146	153	monomer	oligomeric_state	(C) E62A EncFtnsH displays charge states consistent with a decamer (green circles). (D) H65A EncFtnsH displays charge states consistent with both monomer (blue circles) and dimer (purple circles).	FIG
+173	178	dimer	oligomeric_state	(C) E62A EncFtnsH displays charge states consistent with a decamer (green circles). (D) H65A EncFtnsH displays charge states consistent with both monomer (blue circles) and dimer (purple circles).	FIG
+15	18	SEC	experimental_method	In addition to SEC studies, native mass spectrometry of the apo-EncFtnsH mutants was performed and compared with the wild-type apo-EncFtnsH protein (Figure 10).	RESULTS
+28	52	native mass spectrometry	experimental_method	In addition to SEC studies, native mass spectrometry of the apo-EncFtnsH mutants was performed and compared with the wild-type apo-EncFtnsH protein (Figure 10).	RESULTS
+60	63	apo	protein_state	In addition to SEC studies, native mass spectrometry of the apo-EncFtnsH mutants was performed and compared with the wild-type apo-EncFtnsH protein (Figure 10).	RESULTS
+64	72	EncFtnsH	protein	In addition to SEC studies, native mass spectrometry of the apo-EncFtnsH mutants was performed and compared with the wild-type apo-EncFtnsH protein (Figure 10).	RESULTS
+73	80	mutants	protein_state	In addition to SEC studies, native mass spectrometry of the apo-EncFtnsH mutants was performed and compared with the wild-type apo-EncFtnsH protein (Figure 10).	RESULTS
+117	126	wild-type	protein_state	In addition to SEC studies, native mass spectrometry of the apo-EncFtnsH mutants was performed and compared with the wild-type apo-EncFtnsH protein (Figure 10).	RESULTS
+127	130	apo	protein_state	In addition to SEC studies, native mass spectrometry of the apo-EncFtnsH mutants was performed and compared with the wild-type apo-EncFtnsH protein (Figure 10).	RESULTS
+131	139	EncFtnsH	protein	In addition to SEC studies, native mass spectrometry of the apo-EncFtnsH mutants was performed and compared with the wild-type apo-EncFtnsH protein (Figure 10).	RESULTS
+24	27	apo	protein_state	As described above, the apo-EncFtnsH has a charge state distribution consistent with an unstructured monomer, and decamer formation is only initiated upon addition of ferrous iron.	RESULTS
+28	36	EncFtnsH	protein	As described above, the apo-EncFtnsH has a charge state distribution consistent with an unstructured monomer, and decamer formation is only initiated upon addition of ferrous iron.	RESULTS
+43	55	charge state	evidence	As described above, the apo-EncFtnsH has a charge state distribution consistent with an unstructured monomer, and decamer formation is only initiated upon addition of ferrous iron.	RESULTS
+88	100	unstructured	protein_state	As described above, the apo-EncFtnsH has a charge state distribution consistent with an unstructured monomer, and decamer formation is only initiated upon addition of ferrous iron.	RESULTS
+101	108	monomer	oligomeric_state	As described above, the apo-EncFtnsH has a charge state distribution consistent with an unstructured monomer, and decamer formation is only initiated upon addition of ferrous iron.	RESULTS
+114	121	decamer	oligomeric_state	As described above, the apo-EncFtnsH has a charge state distribution consistent with an unstructured monomer, and decamer formation is only initiated upon addition of ferrous iron.	RESULTS
+175	179	iron	chemical	As described above, the apo-EncFtnsH has a charge state distribution consistent with an unstructured monomer, and decamer formation is only initiated upon addition of ferrous iron.	RESULTS
+9	13	E32A	mutant	Both the E32A mutant and E62A mutant displayed charge state distributions consistent with decamers, even in the absence of Fe2+.	RESULTS
+14	20	mutant	protein_state	Both the E32A mutant and E62A mutant displayed charge state distributions consistent with decamers, even in the absence of Fe2+.	RESULTS
+25	29	E62A	mutant	Both the E32A mutant and E62A mutant displayed charge state distributions consistent with decamers, even in the absence of Fe2+.	RESULTS
+30	36	mutant	protein_state	Both the E32A mutant and E62A mutant displayed charge state distributions consistent with decamers, even in the absence of Fe2+.	RESULTS
+47	59	charge state	evidence	Both the E32A mutant and E62A mutant displayed charge state distributions consistent with decamers, even in the absence of Fe2+.	RESULTS
+90	98	decamers	oligomeric_state	Both the E32A mutant and E62A mutant displayed charge state distributions consistent with decamers, even in the absence of Fe2+.	RESULTS
+112	122	absence of	protein_state	Both the E32A mutant and E62A mutant displayed charge state distributions consistent with decamers, even in the absence of Fe2+.	RESULTS
+123	127	Fe2+	chemical	Both the E32A mutant and E62A mutant displayed charge state distributions consistent with decamers, even in the absence of Fe2+.	RESULTS
+46	49	SEC	experimental_method	This gas-phase observation is consistent with SEC measurements, which indicate both of these variants were also decamers in solution.	RESULTS
+112	120	decamers	oligomeric_state	This gas-phase observation is consistent with SEC measurements, which indicate both of these variants were also decamers in solution.	RESULTS
+45	52	decamer	oligomeric_state	Thus it seems that these mutations allow the decamer to form in the absence of iron in the FOC.	RESULTS
+68	78	absence of	protein_state	Thus it seems that these mutations allow the decamer to form in the absence of iron in the FOC.	RESULTS
+79	83	iron	chemical	Thus it seems that these mutations allow the decamer to form in the absence of iron in the FOC.	RESULTS
+91	94	FOC	site	Thus it seems that these mutations allow the decamer to form in the absence of iron in the FOC.	RESULTS
+19	32	glutamic acid	residue_name	In contrast to the glutamic acid mutants, MS analysis of the H65A mutant is similar to wild-type apo-EncFtnsH and is present as a monomer; interestingly a minor population of dimeric H65A was also observed.	RESULTS
+33	40	mutants	protein_state	In contrast to the glutamic acid mutants, MS analysis of the H65A mutant is similar to wild-type apo-EncFtnsH and is present as a monomer; interestingly a minor population of dimeric H65A was also observed.	RESULTS
+42	44	MS	experimental_method	In contrast to the glutamic acid mutants, MS analysis of the H65A mutant is similar to wild-type apo-EncFtnsH and is present as a monomer; interestingly a minor population of dimeric H65A was also observed.	RESULTS
+61	65	H65A	mutant	In contrast to the glutamic acid mutants, MS analysis of the H65A mutant is similar to wild-type apo-EncFtnsH and is present as a monomer; interestingly a minor population of dimeric H65A was also observed.	RESULTS
+66	72	mutant	protein_state	In contrast to the glutamic acid mutants, MS analysis of the H65A mutant is similar to wild-type apo-EncFtnsH and is present as a monomer; interestingly a minor population of dimeric H65A was also observed.	RESULTS
+87	96	wild-type	protein_state	In contrast to the glutamic acid mutants, MS analysis of the H65A mutant is similar to wild-type apo-EncFtnsH and is present as a monomer; interestingly a minor population of dimeric H65A was also observed.	RESULTS
+97	100	apo	protein_state	In contrast to the glutamic acid mutants, MS analysis of the H65A mutant is similar to wild-type apo-EncFtnsH and is present as a monomer; interestingly a minor population of dimeric H65A was also observed.	RESULTS
+101	109	EncFtnsH	protein	In contrast to the glutamic acid mutants, MS analysis of the H65A mutant is similar to wild-type apo-EncFtnsH and is present as a monomer; interestingly a minor population of dimeric H65A was also observed.	RESULTS
+130	137	monomer	oligomeric_state	In contrast to the glutamic acid mutants, MS analysis of the H65A mutant is similar to wild-type apo-EncFtnsH and is present as a monomer; interestingly a minor population of dimeric H65A was also observed.	RESULTS
+175	182	dimeric	oligomeric_state	In contrast to the glutamic acid mutants, MS analysis of the H65A mutant is similar to wild-type apo-EncFtnsH and is present as a monomer; interestingly a minor population of dimeric H65A was also observed.	RESULTS
+183	187	H65A	mutant	In contrast to the glutamic acid mutants, MS analysis of the H65A mutant is similar to wild-type apo-EncFtnsH and is present as a monomer; interestingly a minor population of dimeric H65A was also observed.	RESULTS
+77	81	E32A	mutant	We propose that the observed differences in the oligomerization state of the E32A and E62A mutants compared to wild-type are due to the changes in the electrostatic environment within the FOC.	RESULTS
+86	90	E62A	mutant	We propose that the observed differences in the oligomerization state of the E32A and E62A mutants compared to wild-type are due to the changes in the electrostatic environment within the FOC.	RESULTS
+91	98	mutants	protein_state	We propose that the observed differences in the oligomerization state of the E32A and E62A mutants compared to wild-type are due to the changes in the electrostatic environment within the FOC.	RESULTS
+111	120	wild-type	protein_state	We propose that the observed differences in the oligomerization state of the E32A and E62A mutants compared to wild-type are due to the changes in the electrostatic environment within the FOC.	RESULTS
+188	191	FOC	site	We propose that the observed differences in the oligomerization state of the E32A and E62A mutants compared to wild-type are due to the changes in the electrostatic environment within the FOC.	RESULTS
+3	13	neutral pH	protein_state	At neutral pH the glutamic acid residues are negatively charged, while the histidine residues are predominantly in their uncharged state.	RESULTS
+18	31	glutamic acid	residue_name	At neutral pH the glutamic acid residues are negatively charged, while the histidine residues are predominantly in their uncharged state.	RESULTS
+75	84	histidine	residue_name	At neutral pH the glutamic acid residues are negatively charged, while the histidine residues are predominantly in their uncharged state.	RESULTS
+7	16	wild-type	protein_state	In the wild-type (WT) EncFtnsH this leads to electrostatic repulsion between subunits in the absence of iron.	RESULTS
+18	20	WT	protein_state	In the wild-type (WT) EncFtnsH this leads to electrostatic repulsion between subunits in the absence of iron.	RESULTS
+22	30	EncFtnsH	protein	In the wild-type (WT) EncFtnsH this leads to electrostatic repulsion between subunits in the absence of iron.	RESULTS
+77	85	subunits	structure_element	In the wild-type (WT) EncFtnsH this leads to electrostatic repulsion between subunits in the absence of iron.	RESULTS
+93	103	absence of	protein_state	In the wild-type (WT) EncFtnsH this leads to electrostatic repulsion between subunits in the absence of iron.	RESULTS
+104	108	iron	chemical	In the wild-type (WT) EncFtnsH this leads to electrostatic repulsion between subunits in the absence of iron.	RESULTS
+0	12	Coordination	bond_interaction	Coordination of Fe2+ in this site stabilizes the dimer and reconstitutes the active FOC.	RESULTS
+16	20	Fe2+	chemical	Coordination of Fe2+ in this site stabilizes the dimer and reconstitutes the active FOC.	RESULTS
+49	54	dimer	oligomeric_state	Coordination of Fe2+ in this site stabilizes the dimer and reconstitutes the active FOC.	RESULTS
+77	83	active	protein_state	Coordination of Fe2+ in this site stabilizes the dimer and reconstitutes the active FOC.	RESULTS
+84	87	FOC	site	Coordination of Fe2+ in this site stabilizes the dimer and reconstitutes the active FOC.	RESULTS
+29	34	Glu32	residue_name_number	The geometric arrangement of Glu32 and Glu62 in the FOC explains their behavior in solution and the gas phase, where they both favor the formation of decamers due to the loss of a repulsive negative charge.	RESULTS
+39	44	Glu62	residue_name_number	The geometric arrangement of Glu32 and Glu62 in the FOC explains their behavior in solution and the gas phase, where they both favor the formation of decamers due to the loss of a repulsive negative charge.	RESULTS
+52	55	FOC	site	The geometric arrangement of Glu32 and Glu62 in the FOC explains their behavior in solution and the gas phase, where they both favor the formation of decamers due to the loss of a repulsive negative charge.	RESULTS
+150	158	decamers	oligomeric_state	The geometric arrangement of Glu32 and Glu62 in the FOC explains their behavior in solution and the gas phase, where they both favor the formation of decamers due to the loss of a repulsive negative charge.	RESULTS
+4	7	FOC	site	The FOC in the H65A mutant is destabilized through the loss of this metal coordinating residue and potential positive charge carrier, thus favoring the monomer in solution and the gas phase.	RESULTS
+15	19	H65A	mutant	The FOC in the H65A mutant is destabilized through the loss of this metal coordinating residue and potential positive charge carrier, thus favoring the monomer in solution and the gas phase.	RESULTS
+20	26	mutant	protein_state	The FOC in the H65A mutant is destabilized through the loss of this metal coordinating residue and potential positive charge carrier, thus favoring the monomer in solution and the gas phase.	RESULTS
+55	62	loss of	protein_state	The FOC in the H65A mutant is destabilized through the loss of this metal coordinating residue and potential positive charge carrier, thus favoring the monomer in solution and the gas phase.	RESULTS
+68	94	metal coordinating residue	site	The FOC in the H65A mutant is destabilized through the loss of this metal coordinating residue and potential positive charge carrier, thus favoring the monomer in solution and the gas phase.	RESULTS
+152	159	monomer	oligomeric_state	The FOC in the H65A mutant is destabilized through the loss of this metal coordinating residue and potential positive charge carrier, thus favoring the monomer in solution and the gas phase.	RESULTS
+0	41	Data collection and refinement statistics	evidence	Data collection and refinement statistics.	TABLE
+1	3	WT	protein_state	"	WT	E32A	E62A	H65A	 	Data collection					 	Wavelength (Å)	1.74	1.73	1.73	1.74	 	Resolution range (Å)	49.63 - 2.06 (2.10 - 2.06)	48.84 - 2.59 (2.683 - 2.59)	48.87 - 2.21 (2.29 - 2.21)	48.86 - 2.97 (3.08 - 2.97)	 	Space group	P 1 21 1	P 1 21 1	P 1 21 1	P 1 21 1	 	Unit cell (Å) a b  c β (°)	98.18 120.53 140.30 95.36	97.78 120.28 140.53 95.41	98.09 120.23 140.36 95.50	98.03 120.29 140.43 95.39	 	Total reflections	1,264,922 (41,360)	405,488 (36,186)	1,069,345 (95,716)	323,853 (32,120)	 	Unique reflections	197,873 (8,766)	100,067 (9,735)	162,379 (15,817)	66,658 (6,553)	 	Multiplicity	6.4 (4.7)	4.1 (3.7)	6.6 (6.1)	4.9 (4.9)	 	Anomalous multiplicity	3.2 (2.6)	N/A	N/A	N/A	 	Completeness (%)	99.2 (88.6)	99.0 (97.0)	100 (97.0)	100 (99.0)	 	Anomalous completeness (%)	96.7 (77.2)	N/A	N/A	N/A	 	Mean I/sigma(I)	10.6 (1.60)	8.46 (1.79)	13.74 (1.80)	8.09 (1.74)	 	Wilson B-factor	26.98	40.10	33.97	52.20	 	Rmerge	0.123 (0.790)	0.171 (0.792)	0.0979 (1.009)	0.177 (0.863)	 	Rmeas	0.147 (0.973)	0.196 (0.923)	0.1064 (1.107)	0.199 (0.966)	 	CC1/2	0.995 (0.469)	0.985 (0.557)	0.998 (0.642)	0.989 (0.627)	 	CC*	0.999 (0.846)	0.996 (0.846)	0.999 (0.884)	0.997 (0.878)	 	Image DOI	10.7488/ds/1342	10.7488/ds/1419	10.7488/ds/1420	10.7488/ds/1421	 	Refinement					 	Rwork	0.171 (0.318)	0.183 (0.288)	0.165 (0.299)	0.186 (0.273)	 	Rfree	0.206 (0.345)	0.225 (0351)	0.216 (0.364)	0.237 (0.325)	 	Number of non-hydrogen atoms	23,222	22,366	22,691	22,145	 	macromolecules	22,276	22,019	21,965	22,066	 	ligands	138	8	24	74	 	water	808	339	702	5	 	Protein residues	2,703	2,686	2,675	2,700	 	RMS(bonds) (Å)	0.012	0.005	0.011	0.002	 	RMS(angles) (°)	1.26	0.58	1.02	0.40	 	Ramachandran favored (%)	100	99	100	99	 	Ramachandran allowed (%)	0	1	0	1	 	Ramachandran outliers (%)	0	0	0	0	 	Clash score	1.42	1.42	1.79	0.97	 	Average B-factor (Å2)	33.90	42.31	41.34	47.68	 	macromolecules	33.80	42.35	41.31	47.60	 	ligands	40.40	72.80	65.55	72.34	 	solvent	36.20	38.95	41.46	33.85	 	PDB ID	5DA5	5L89	5L8B	5L8G	 	"	TABLE
+4	8	E32A	mutant	"	WT	E32A	E62A	H65A	 	Data collection					 	Wavelength (Å)	1.74	1.73	1.73	1.74	 	Resolution range (Å)	49.63 - 2.06 (2.10 - 2.06)	48.84 - 2.59 (2.683 - 2.59)	48.87 - 2.21 (2.29 - 2.21)	48.86 - 2.97 (3.08 - 2.97)	 	Space group	P 1 21 1	P 1 21 1	P 1 21 1	P 1 21 1	 	Unit cell (Å) a b  c β (°)	98.18 120.53 140.30 95.36	97.78 120.28 140.53 95.41	98.09 120.23 140.36 95.50	98.03 120.29 140.43 95.39	 	Total reflections	1,264,922 (41,360)	405,488 (36,186)	1,069,345 (95,716)	323,853 (32,120)	 	Unique reflections	197,873 (8,766)	100,067 (9,735)	162,379 (15,817)	66,658 (6,553)	 	Multiplicity	6.4 (4.7)	4.1 (3.7)	6.6 (6.1)	4.9 (4.9)	 	Anomalous multiplicity	3.2 (2.6)	N/A	N/A	N/A	 	Completeness (%)	99.2 (88.6)	99.0 (97.0)	100 (97.0)	100 (99.0)	 	Anomalous completeness (%)	96.7 (77.2)	N/A	N/A	N/A	 	Mean I/sigma(I)	10.6 (1.60)	8.46 (1.79)	13.74 (1.80)	8.09 (1.74)	 	Wilson B-factor	26.98	40.10	33.97	52.20	 	Rmerge	0.123 (0.790)	0.171 (0.792)	0.0979 (1.009)	0.177 (0.863)	 	Rmeas	0.147 (0.973)	0.196 (0.923)	0.1064 (1.107)	0.199 (0.966)	 	CC1/2	0.995 (0.469)	0.985 (0.557)	0.998 (0.642)	0.989 (0.627)	 	CC*	0.999 (0.846)	0.996 (0.846)	0.999 (0.884)	0.997 (0.878)	 	Image DOI	10.7488/ds/1342	10.7488/ds/1419	10.7488/ds/1420	10.7488/ds/1421	 	Refinement					 	Rwork	0.171 (0.318)	0.183 (0.288)	0.165 (0.299)	0.186 (0.273)	 	Rfree	0.206 (0.345)	0.225 (0351)	0.216 (0.364)	0.237 (0.325)	 	Number of non-hydrogen atoms	23,222	22,366	22,691	22,145	 	macromolecules	22,276	22,019	21,965	22,066	 	ligands	138	8	24	74	 	water	808	339	702	5	 	Protein residues	2,703	2,686	2,675	2,700	 	RMS(bonds) (Å)	0.012	0.005	0.011	0.002	 	RMS(angles) (°)	1.26	0.58	1.02	0.40	 	Ramachandran favored (%)	100	99	100	99	 	Ramachandran allowed (%)	0	1	0	1	 	Ramachandran outliers (%)	0	0	0	0	 	Clash score	1.42	1.42	1.79	0.97	 	Average B-factor (Å2)	33.90	42.31	41.34	47.68	 	macromolecules	33.80	42.35	41.31	47.60	 	ligands	40.40	72.80	65.55	72.34	 	solvent	36.20	38.95	41.46	33.85	 	PDB ID	5DA5	5L89	5L8B	5L8G	 	"	TABLE
+9	13	E62A	mutant	"	WT	E32A	E62A	H65A	 	Data collection					 	Wavelength (Å)	1.74	1.73	1.73	1.74	 	Resolution range (Å)	49.63 - 2.06 (2.10 - 2.06)	48.84 - 2.59 (2.683 - 2.59)	48.87 - 2.21 (2.29 - 2.21)	48.86 - 2.97 (3.08 - 2.97)	 	Space group	P 1 21 1	P 1 21 1	P 1 21 1	P 1 21 1	 	Unit cell (Å) a b  c β (°)	98.18 120.53 140.30 95.36	97.78 120.28 140.53 95.41	98.09 120.23 140.36 95.50	98.03 120.29 140.43 95.39	 	Total reflections	1,264,922 (41,360)	405,488 (36,186)	1,069,345 (95,716)	323,853 (32,120)	 	Unique reflections	197,873 (8,766)	100,067 (9,735)	162,379 (15,817)	66,658 (6,553)	 	Multiplicity	6.4 (4.7)	4.1 (3.7)	6.6 (6.1)	4.9 (4.9)	 	Anomalous multiplicity	3.2 (2.6)	N/A	N/A	N/A	 	Completeness (%)	99.2 (88.6)	99.0 (97.0)	100 (97.0)	100 (99.0)	 	Anomalous completeness (%)	96.7 (77.2)	N/A	N/A	N/A	 	Mean I/sigma(I)	10.6 (1.60)	8.46 (1.79)	13.74 (1.80)	8.09 (1.74)	 	Wilson B-factor	26.98	40.10	33.97	52.20	 	Rmerge	0.123 (0.790)	0.171 (0.792)	0.0979 (1.009)	0.177 (0.863)	 	Rmeas	0.147 (0.973)	0.196 (0.923)	0.1064 (1.107)	0.199 (0.966)	 	CC1/2	0.995 (0.469)	0.985 (0.557)	0.998 (0.642)	0.989 (0.627)	 	CC*	0.999 (0.846)	0.996 (0.846)	0.999 (0.884)	0.997 (0.878)	 	Image DOI	10.7488/ds/1342	10.7488/ds/1419	10.7488/ds/1420	10.7488/ds/1421	 	Refinement					 	Rwork	0.171 (0.318)	0.183 (0.288)	0.165 (0.299)	0.186 (0.273)	 	Rfree	0.206 (0.345)	0.225 (0351)	0.216 (0.364)	0.237 (0.325)	 	Number of non-hydrogen atoms	23,222	22,366	22,691	22,145	 	macromolecules	22,276	22,019	21,965	22,066	 	ligands	138	8	24	74	 	water	808	339	702	5	 	Protein residues	2,703	2,686	2,675	2,700	 	RMS(bonds) (Å)	0.012	0.005	0.011	0.002	 	RMS(angles) (°)	1.26	0.58	1.02	0.40	 	Ramachandran favored (%)	100	99	100	99	 	Ramachandran allowed (%)	0	1	0	1	 	Ramachandran outliers (%)	0	0	0	0	 	Clash score	1.42	1.42	1.79	0.97	 	Average B-factor (Å2)	33.90	42.31	41.34	47.68	 	macromolecules	33.80	42.35	41.31	47.60	 	ligands	40.40	72.80	65.55	72.34	 	solvent	36.20	38.95	41.46	33.85	 	PDB ID	5DA5	5L89	5L8B	5L8G	 	"	TABLE
+14	18	H65A	mutant	"	WT	E32A	E62A	H65A	 	Data collection					 	Wavelength (Å)	1.74	1.73	1.73	1.74	 	Resolution range (Å)	49.63 - 2.06 (2.10 - 2.06)	48.84 - 2.59 (2.683 - 2.59)	48.87 - 2.21 (2.29 - 2.21)	48.86 - 2.97 (3.08 - 2.97)	 	Space group	P 1 21 1	P 1 21 1	P 1 21 1	P 1 21 1	 	Unit cell (Å) a b  c β (°)	98.18 120.53 140.30 95.36	97.78 120.28 140.53 95.41	98.09 120.23 140.36 95.50	98.03 120.29 140.43 95.39	 	Total reflections	1,264,922 (41,360)	405,488 (36,186)	1,069,345 (95,716)	323,853 (32,120)	 	Unique reflections	197,873 (8,766)	100,067 (9,735)	162,379 (15,817)	66,658 (6,553)	 	Multiplicity	6.4 (4.7)	4.1 (3.7)	6.6 (6.1)	4.9 (4.9)	 	Anomalous multiplicity	3.2 (2.6)	N/A	N/A	N/A	 	Completeness (%)	99.2 (88.6)	99.0 (97.0)	100 (97.0)	100 (99.0)	 	Anomalous completeness (%)	96.7 (77.2)	N/A	N/A	N/A	 	Mean I/sigma(I)	10.6 (1.60)	8.46 (1.79)	13.74 (1.80)	8.09 (1.74)	 	Wilson B-factor	26.98	40.10	33.97	52.20	 	Rmerge	0.123 (0.790)	0.171 (0.792)	0.0979 (1.009)	0.177 (0.863)	 	Rmeas	0.147 (0.973)	0.196 (0.923)	0.1064 (1.107)	0.199 (0.966)	 	CC1/2	0.995 (0.469)	0.985 (0.557)	0.998 (0.642)	0.989 (0.627)	 	CC*	0.999 (0.846)	0.996 (0.846)	0.999 (0.884)	0.997 (0.878)	 	Image DOI	10.7488/ds/1342	10.7488/ds/1419	10.7488/ds/1420	10.7488/ds/1421	 	Refinement					 	Rwork	0.171 (0.318)	0.183 (0.288)	0.165 (0.299)	0.186 (0.273)	 	Rfree	0.206 (0.345)	0.225 (0351)	0.216 (0.364)	0.237 (0.325)	 	Number of non-hydrogen atoms	23,222	22,366	22,691	22,145	 	macromolecules	22,276	22,019	21,965	22,066	 	ligands	138	8	24	74	 	water	808	339	702	5	 	Protein residues	2,703	2,686	2,675	2,700	 	RMS(bonds) (Å)	0.012	0.005	0.011	0.002	 	RMS(angles) (°)	1.26	0.58	1.02	0.40	 	Ramachandran favored (%)	100	99	100	99	 	Ramachandran allowed (%)	0	1	0	1	 	Ramachandran outliers (%)	0	0	0	0	 	Clash score	1.42	1.42	1.79	0.97	 	Average B-factor (Å2)	33.90	42.31	41.34	47.68	 	macromolecules	33.80	42.35	41.31	47.60	 	ligands	40.40	72.80	65.55	72.34	 	solvent	36.20	38.95	41.46	33.85	 	PDB ID	5DA5	5L89	5L8B	5L8G	 	"	TABLE
+1504	1509	water	chemical	"	WT	E32A	E62A	H65A	 	Data collection					 	Wavelength (Å)	1.74	1.73	1.73	1.74	 	Resolution range (Å)	49.63 - 2.06 (2.10 - 2.06)	48.84 - 2.59 (2.683 - 2.59)	48.87 - 2.21 (2.29 - 2.21)	48.86 - 2.97 (3.08 - 2.97)	 	Space group	P 1 21 1	P 1 21 1	P 1 21 1	P 1 21 1	 	Unit cell (Å) a b  c β (°)	98.18 120.53 140.30 95.36	97.78 120.28 140.53 95.41	98.09 120.23 140.36 95.50	98.03 120.29 140.43 95.39	 	Total reflections	1,264,922 (41,360)	405,488 (36,186)	1,069,345 (95,716)	323,853 (32,120)	 	Unique reflections	197,873 (8,766)	100,067 (9,735)	162,379 (15,817)	66,658 (6,553)	 	Multiplicity	6.4 (4.7)	4.1 (3.7)	6.6 (6.1)	4.9 (4.9)	 	Anomalous multiplicity	3.2 (2.6)	N/A	N/A	N/A	 	Completeness (%)	99.2 (88.6)	99.0 (97.0)	100 (97.0)	100 (99.0)	 	Anomalous completeness (%)	96.7 (77.2)	N/A	N/A	N/A	 	Mean I/sigma(I)	10.6 (1.60)	8.46 (1.79)	13.74 (1.80)	8.09 (1.74)	 	Wilson B-factor	26.98	40.10	33.97	52.20	 	Rmerge	0.123 (0.790)	0.171 (0.792)	0.0979 (1.009)	0.177 (0.863)	 	Rmeas	0.147 (0.973)	0.196 (0.923)	0.1064 (1.107)	0.199 (0.966)	 	CC1/2	0.995 (0.469)	0.985 (0.557)	0.998 (0.642)	0.989 (0.627)	 	CC*	0.999 (0.846)	0.996 (0.846)	0.999 (0.884)	0.997 (0.878)	 	Image DOI	10.7488/ds/1342	10.7488/ds/1419	10.7488/ds/1420	10.7488/ds/1421	 	Refinement					 	Rwork	0.171 (0.318)	0.183 (0.288)	0.165 (0.299)	0.186 (0.273)	 	Rfree	0.206 (0.345)	0.225 (0351)	0.216 (0.364)	0.237 (0.325)	 	Number of non-hydrogen atoms	23,222	22,366	22,691	22,145	 	macromolecules	22,276	22,019	21,965	22,066	 	ligands	138	8	24	74	 	water	808	339	702	5	 	Protein residues	2,703	2,686	2,675	2,700	 	RMS(bonds) (Å)	0.012	0.005	0.011	0.002	 	RMS(angles) (°)	1.26	0.58	1.02	0.40	 	Ramachandran favored (%)	100	99	100	99	 	Ramachandran allowed (%)	0	1	0	1	 	Ramachandran outliers (%)	0	0	0	0	 	Clash score	1.42	1.42	1.79	0.97	 	Average B-factor (Å2)	33.90	42.31	41.34	47.68	 	macromolecules	33.80	42.35	41.31	47.60	 	ligands	40.40	72.80	65.55	72.34	 	solvent	36.20	38.95	41.46	33.85	 	PDB ID	5DA5	5L89	5L8B	5L8G	 	"	TABLE
+0	4	Iron	chemical	Iron loading capacity of EncFtn, encapsulin and ferritin.	TABLE
+25	31	EncFtn	protein	Iron loading capacity of EncFtn, encapsulin and ferritin.	TABLE
+33	43	encapsulin	protein	Iron loading capacity of EncFtn, encapsulin and ferritin.	TABLE
+48	56	ferritin	protein_type	Iron loading capacity of EncFtn, encapsulin and ferritin.	TABLE
+38	47	decameric	oligomeric_state	Protein samples (at 8.5 µM) including decameric EncFtnsH, encapsulin, EncFtn-Enc and apoferritin were mixed with Fe(NH4)2(SO4) (in 0.1% (v/v) HCl) of different concentrations in 50 mM Tris-HCl (pH 8.0), 150 mM NaCl buffer at room temperature for 3 hrs in the air.	TABLE
+48	56	EncFtnsH	protein	Protein samples (at 8.5 µM) including decameric EncFtnsH, encapsulin, EncFtn-Enc and apoferritin were mixed with Fe(NH4)2(SO4) (in 0.1% (v/v) HCl) of different concentrations in 50 mM Tris-HCl (pH 8.0), 150 mM NaCl buffer at room temperature for 3 hrs in the air.	TABLE
+58	68	encapsulin	protein	Protein samples (at 8.5 µM) including decameric EncFtnsH, encapsulin, EncFtn-Enc and apoferritin were mixed with Fe(NH4)2(SO4) (in 0.1% (v/v) HCl) of different concentrations in 50 mM Tris-HCl (pH 8.0), 150 mM NaCl buffer at room temperature for 3 hrs in the air.	TABLE
+70	80	EncFtn-Enc	complex_assembly	Protein samples (at 8.5 µM) including decameric EncFtnsH, encapsulin, EncFtn-Enc and apoferritin were mixed with Fe(NH4)2(SO4) (in 0.1% (v/v) HCl) of different concentrations in 50 mM Tris-HCl (pH 8.0), 150 mM NaCl buffer at room temperature for 3 hrs in the air.	TABLE
+85	96	apoferritin	protein_state	Protein samples (at 8.5 µM) including decameric EncFtnsH, encapsulin, EncFtn-Enc and apoferritin were mixed with Fe(NH4)2(SO4) (in 0.1% (v/v) HCl) of different concentrations in 50 mM Tris-HCl (pH 8.0), 150 mM NaCl buffer at room temperature for 3 hrs in the air.	TABLE
+113	126	Fe(NH4)2(SO4)	chemical	Protein samples (at 8.5 µM) including decameric EncFtnsH, encapsulin, EncFtn-Enc and apoferritin were mixed with Fe(NH4)2(SO4) (in 0.1% (v/v) HCl) of different concentrations in 50 mM Tris-HCl (pH 8.0), 150 mM NaCl buffer at room temperature for 3 hrs in the air.	TABLE
+142	145	HCl	chemical	Protein samples (at 8.5 µM) including decameric EncFtnsH, encapsulin, EncFtn-Enc and apoferritin were mixed with Fe(NH4)2(SO4) (in 0.1% (v/v) HCl) of different concentrations in 50 mM Tris-HCl (pH 8.0), 150 mM NaCl buffer at room temperature for 3 hrs in the air.	TABLE
+210	214	NaCl	chemical	Protein samples (at 8.5 µM) including decameric EncFtnsH, encapsulin, EncFtn-Enc and apoferritin were mixed with Fe(NH4)2(SO4) (in 0.1% (v/v) HCl) of different concentrations in 50 mM Tris-HCl (pH 8.0), 150 mM NaCl buffer at room temperature for 3 hrs in the air.	TABLE
+8	10	Fe	chemical	Protein-Fe mixtures were centrifuged at 13,000 x g to remove precipitated material and desalted prior to the Fe and protein content analysis by ferrozine assay and BCA microplate assay, respectively.	TABLE
+109	111	Fe	chemical	Protein-Fe mixtures were centrifuged at 13,000 x g to remove precipitated material and desalted prior to the Fe and protein content analysis by ferrozine assay and BCA microplate assay, respectively.	TABLE
+144	159	ferrozine assay	experimental_method	Protein-Fe mixtures were centrifuged at 13,000 x g to remove precipitated material and desalted prior to the Fe and protein content analysis by ferrozine assay and BCA microplate assay, respectively.	TABLE
+164	184	BCA microplate assay	experimental_method	Protein-Fe mixtures were centrifuged at 13,000 x g to remove precipitated material and desalted prior to the Fe and protein content analysis by ferrozine assay and BCA microplate assay, respectively.	TABLE
+0	2	Fe	chemical	Fe to protein ratio was calculated to indicate the Fe binding capacity of the protein.	TABLE
+51	53	Fe	chemical	Fe to protein ratio was calculated to indicate the Fe binding capacity of the protein.	TABLE
+42	46	iron	chemical	Protein stability was compromised at high iron concentrations; therefore, the highest iron loading with the least protein precipitation was used to derive the maximum iron loading capacity per biological assembly (underlined and highlighted in bold).	TABLE
+86	90	iron	chemical	Protein stability was compromised at high iron concentrations; therefore, the highest iron loading with the least protein precipitation was used to derive the maximum iron loading capacity per biological assembly (underlined and highlighted in bold).	TABLE
+167	171	iron	chemical	Protein stability was compromised at high iron concentrations; therefore, the highest iron loading with the least protein precipitation was used to derive the maximum iron loading capacity per biological assembly (underlined and highlighted in bold).	TABLE
+37	44	decamer	oligomeric_state	The biological unit assemblies are a decamer for EncFtnsH, a 60mer for encapsulin, a 60mer of encapsulin loaded with 12 copies of decameric EncFtn in the complex, and 24mer for horse spleen apoferritin.	TABLE
+49	57	EncFtnsH	protein	The biological unit assemblies are a decamer for EncFtnsH, a 60mer for encapsulin, a 60mer of encapsulin loaded with 12 copies of decameric EncFtn in the complex, and 24mer for horse spleen apoferritin.	TABLE
+61	66	60mer	oligomeric_state	The biological unit assemblies are a decamer for EncFtnsH, a 60mer for encapsulin, a 60mer of encapsulin loaded with 12 copies of decameric EncFtn in the complex, and 24mer for horse spleen apoferritin.	TABLE
+71	81	encapsulin	protein	The biological unit assemblies are a decamer for EncFtnsH, a 60mer for encapsulin, a 60mer of encapsulin loaded with 12 copies of decameric EncFtn in the complex, and 24mer for horse spleen apoferritin.	TABLE
+85	90	60mer	oligomeric_state	The biological unit assemblies are a decamer for EncFtnsH, a 60mer for encapsulin, a 60mer of encapsulin loaded with 12 copies of decameric EncFtn in the complex, and 24mer for horse spleen apoferritin.	TABLE
+94	104	encapsulin	protein	The biological unit assemblies are a decamer for EncFtnsH, a 60mer for encapsulin, a 60mer of encapsulin loaded with 12 copies of decameric EncFtn in the complex, and 24mer for horse spleen apoferritin.	TABLE
+105	116	loaded with	protein_state	The biological unit assemblies are a decamer for EncFtnsH, a 60mer for encapsulin, a 60mer of encapsulin loaded with 12 copies of decameric EncFtn in the complex, and 24mer for horse spleen apoferritin.	TABLE
+130	139	decameric	oligomeric_state	The biological unit assemblies are a decamer for EncFtnsH, a 60mer for encapsulin, a 60mer of encapsulin loaded with 12 copies of decameric EncFtn in the complex, and 24mer for horse spleen apoferritin.	TABLE
+140	146	EncFtn	protein	The biological unit assemblies are a decamer for EncFtnsH, a 60mer for encapsulin, a 60mer of encapsulin loaded with 12 copies of decameric EncFtn in the complex, and 24mer for horse spleen apoferritin.	TABLE
+167	172	24mer	oligomeric_state	The biological unit assemblies are a decamer for EncFtnsH, a 60mer for encapsulin, a 60mer of encapsulin loaded with 12 copies of decameric EncFtn in the complex, and 24mer for horse spleen apoferritin.	TABLE
+177	182	horse	taxonomy_domain	The biological unit assemblies are a decamer for EncFtnsH, a 60mer for encapsulin, a 60mer of encapsulin loaded with 12 copies of decameric EncFtn in the complex, and 24mer for horse spleen apoferritin.	TABLE
+190	201	apoferritin	protein_state	The biological unit assemblies are a decamer for EncFtnsH, a 60mer for encapsulin, a 60mer of encapsulin loaded with 12 copies of decameric EncFtn in the complex, and 24mer for horse spleen apoferritin.	TABLE
+83	118	ferrozine and BCA microplate assays	experimental_method	Errors are quoted as the standard deviation of three technical repeats in both the ferrozine and BCA microplate assays.	TABLE
+21	23	Fe	chemical	The proteins used in Fe loading experiment came from a single preparation.	TABLE
+15	29	Fe(NH4)2(SO4)2	chemical	"Protein sample	Fe(NH4)2(SO4)2 loading (µM)	Fe detected by ferrozine assay (µM)	Protein detected by BCA microplate assay (µM)	Fe / monomeric protein	Maximum Fe loading per biological assembly unit	 	8.46 µM EncFtnsH-10mer	0	4.73 ± 2.32	5.26 ± 0.64	0.90 ± 0.44		 	39.9	9.93 ± 1.20	5.36 ± 0.69	1.85 ± 0.22		 	84	17.99 ± 2.01	4.96 ± 0.04	3.63 ± 0.41		 	147	21.09 ± 1.94	4.44 ± 0.21	4.75 ± 0.44	48 ± 4	 	224	28.68 ± 0.30	3.73 ± 0.53	7.68 ± 0.08		 	301	11.27 ± 1.10	2.50 ± 0.05	4.51 ± 0.44		 	8.50 µM Encapsulin	0	-1.02 ± 0.54	8.63 ± 0.17	-0.12 ± 0.06		 	224	62.24 ± 2.49	10.01 ± 0.58	6.22 ± 0.35		 	301	67.94 ± 3.15	8.69 ± 0.42	7.81 ± 0.36		 	450	107.96 ± 8.88	8.50 ± 0.69	12.71 ± 1.05		 	700	97.51 ± 3.19	7.26 ± 0.20	13.44 ± 0.44		 	1000	308.63 ± 2.06	8.42 ± 0.34	36.66 ± 0.24	2199 ± 15	 	1500	57.09 ± 0.90	1.44 ± 0.21	39.77 ± 0.62		 	2000	9.2 ± 1.16	0.21 ± 0.14	44.73 ± 5.63		 	8.70 µM EncFtn-Enc	0	3.31 ± 1.57	6.85 ± 0.07	0.48 ± 0.23		 	224	116.27 ± 3.74	7.63 ± 0.12	15.25 ± 0.49		 	301	132.86 ± 4.03	6.66 ± 0.31	19.96 ± 0.61		 	450	220.57 ± 27.33	6.12 ± 1.07	36.06 ± 4.47		 	700	344.03 ± 40.38	6.94 ± 0.17	49.58 ± 5.82		 	1000	496.00 ± 38.48	7.19 ± 0.08	68.94 ± 5.35	4137 ± 321	 	1500	569.98 ± 73.63	5.73 ± 0.03	99.44 ± 12.84		 	2000	584.30 ± 28.33	4.88 ± 0.22	119.62 ± 5.80		 	8.50 µM Apoferritin	0	3.95 ± 2.26	9.37 ± 0.24	0.42 ± 0.25		 	42.5	10.27 ± 1.12	8.27 ± 0.30	1.24 ± 0.18		 	212.5	44.48 ± 2.76	7.85 ± 0.77	5.67 ± 0.83		 	637.5	160.93 ± 4.27	6.76 ± 0.81	23.79 ± 3.12	571 ± 75	 	1275	114.92 ± 3.17	3.84 ± 0.30	29.91 ± 2.95		 	1700	91.40 ± 3.37	3.14 ± 0.35	29.13 ± 3.86		 	"	TABLE
+43	45	Fe	chemical	"Protein sample	Fe(NH4)2(SO4)2 loading (µM)	Fe detected by ferrozine assay (µM)	Protein detected by BCA microplate assay (µM)	Fe / monomeric protein	Maximum Fe loading per biological assembly unit	 	8.46 µM EncFtnsH-10mer	0	4.73 ± 2.32	5.26 ± 0.64	0.90 ± 0.44		 	39.9	9.93 ± 1.20	5.36 ± 0.69	1.85 ± 0.22		 	84	17.99 ± 2.01	4.96 ± 0.04	3.63 ± 0.41		 	147	21.09 ± 1.94	4.44 ± 0.21	4.75 ± 0.44	48 ± 4	 	224	28.68 ± 0.30	3.73 ± 0.53	7.68 ± 0.08		 	301	11.27 ± 1.10	2.50 ± 0.05	4.51 ± 0.44		 	8.50 µM Encapsulin	0	-1.02 ± 0.54	8.63 ± 0.17	-0.12 ± 0.06		 	224	62.24 ± 2.49	10.01 ± 0.58	6.22 ± 0.35		 	301	67.94 ± 3.15	8.69 ± 0.42	7.81 ± 0.36		 	450	107.96 ± 8.88	8.50 ± 0.69	12.71 ± 1.05		 	700	97.51 ± 3.19	7.26 ± 0.20	13.44 ± 0.44		 	1000	308.63 ± 2.06	8.42 ± 0.34	36.66 ± 0.24	2199 ± 15	 	1500	57.09 ± 0.90	1.44 ± 0.21	39.77 ± 0.62		 	2000	9.2 ± 1.16	0.21 ± 0.14	44.73 ± 5.63		 	8.70 µM EncFtn-Enc	0	3.31 ± 1.57	6.85 ± 0.07	0.48 ± 0.23		 	224	116.27 ± 3.74	7.63 ± 0.12	15.25 ± 0.49		 	301	132.86 ± 4.03	6.66 ± 0.31	19.96 ± 0.61		 	450	220.57 ± 27.33	6.12 ± 1.07	36.06 ± 4.47		 	700	344.03 ± 40.38	6.94 ± 0.17	49.58 ± 5.82		 	1000	496.00 ± 38.48	7.19 ± 0.08	68.94 ± 5.35	4137 ± 321	 	1500	569.98 ± 73.63	5.73 ± 0.03	99.44 ± 12.84		 	2000	584.30 ± 28.33	4.88 ± 0.22	119.62 ± 5.80		 	8.50 µM Apoferritin	0	3.95 ± 2.26	9.37 ± 0.24	0.42 ± 0.25		 	42.5	10.27 ± 1.12	8.27 ± 0.30	1.24 ± 0.18		 	212.5	44.48 ± 2.76	7.85 ± 0.77	5.67 ± 0.83		 	637.5	160.93 ± 4.27	6.76 ± 0.81	23.79 ± 3.12	571 ± 75	 	1275	114.92 ± 3.17	3.84 ± 0.30	29.91 ± 2.95		 	1700	91.40 ± 3.37	3.14 ± 0.35	29.13 ± 3.86		 	"	TABLE
+58	73	ferrozine assay	experimental_method	"Protein sample	Fe(NH4)2(SO4)2 loading (µM)	Fe detected by ferrozine assay (µM)	Protein detected by BCA microplate assay (µM)	Fe / monomeric protein	Maximum Fe loading per biological assembly unit	 	8.46 µM EncFtnsH-10mer	0	4.73 ± 2.32	5.26 ± 0.64	0.90 ± 0.44		 	39.9	9.93 ± 1.20	5.36 ± 0.69	1.85 ± 0.22		 	84	17.99 ± 2.01	4.96 ± 0.04	3.63 ± 0.41		 	147	21.09 ± 1.94	4.44 ± 0.21	4.75 ± 0.44	48 ± 4	 	224	28.68 ± 0.30	3.73 ± 0.53	7.68 ± 0.08		 	301	11.27 ± 1.10	2.50 ± 0.05	4.51 ± 0.44		 	8.50 µM Encapsulin	0	-1.02 ± 0.54	8.63 ± 0.17	-0.12 ± 0.06		 	224	62.24 ± 2.49	10.01 ± 0.58	6.22 ± 0.35		 	301	67.94 ± 3.15	8.69 ± 0.42	7.81 ± 0.36		 	450	107.96 ± 8.88	8.50 ± 0.69	12.71 ± 1.05		 	700	97.51 ± 3.19	7.26 ± 0.20	13.44 ± 0.44		 	1000	308.63 ± 2.06	8.42 ± 0.34	36.66 ± 0.24	2199 ± 15	 	1500	57.09 ± 0.90	1.44 ± 0.21	39.77 ± 0.62		 	2000	9.2 ± 1.16	0.21 ± 0.14	44.73 ± 5.63		 	8.70 µM EncFtn-Enc	0	3.31 ± 1.57	6.85 ± 0.07	0.48 ± 0.23		 	224	116.27 ± 3.74	7.63 ± 0.12	15.25 ± 0.49		 	301	132.86 ± 4.03	6.66 ± 0.31	19.96 ± 0.61		 	450	220.57 ± 27.33	6.12 ± 1.07	36.06 ± 4.47		 	700	344.03 ± 40.38	6.94 ± 0.17	49.58 ± 5.82		 	1000	496.00 ± 38.48	7.19 ± 0.08	68.94 ± 5.35	4137 ± 321	 	1500	569.98 ± 73.63	5.73 ± 0.03	99.44 ± 12.84		 	2000	584.30 ± 28.33	4.88 ± 0.22	119.62 ± 5.80		 	8.50 µM Apoferritin	0	3.95 ± 2.26	9.37 ± 0.24	0.42 ± 0.25		 	42.5	10.27 ± 1.12	8.27 ± 0.30	1.24 ± 0.18		 	212.5	44.48 ± 2.76	7.85 ± 0.77	5.67 ± 0.83		 	637.5	160.93 ± 4.27	6.76 ± 0.81	23.79 ± 3.12	571 ± 75	 	1275	114.92 ± 3.17	3.84 ± 0.30	29.91 ± 2.95		 	1700	91.40 ± 3.37	3.14 ± 0.35	29.13 ± 3.86		 	"	TABLE
+99	119	BCA microplate assay	experimental_method	"Protein sample	Fe(NH4)2(SO4)2 loading (µM)	Fe detected by ferrozine assay (µM)	Protein detected by BCA microplate assay (µM)	Fe / monomeric protein	Maximum Fe loading per biological assembly unit	 	8.46 µM EncFtnsH-10mer	0	4.73 ± 2.32	5.26 ± 0.64	0.90 ± 0.44		 	39.9	9.93 ± 1.20	5.36 ± 0.69	1.85 ± 0.22		 	84	17.99 ± 2.01	4.96 ± 0.04	3.63 ± 0.41		 	147	21.09 ± 1.94	4.44 ± 0.21	4.75 ± 0.44	48 ± 4	 	224	28.68 ± 0.30	3.73 ± 0.53	7.68 ± 0.08		 	301	11.27 ± 1.10	2.50 ± 0.05	4.51 ± 0.44		 	8.50 µM Encapsulin	0	-1.02 ± 0.54	8.63 ± 0.17	-0.12 ± 0.06		 	224	62.24 ± 2.49	10.01 ± 0.58	6.22 ± 0.35		 	301	67.94 ± 3.15	8.69 ± 0.42	7.81 ± 0.36		 	450	107.96 ± 8.88	8.50 ± 0.69	12.71 ± 1.05		 	700	97.51 ± 3.19	7.26 ± 0.20	13.44 ± 0.44		 	1000	308.63 ± 2.06	8.42 ± 0.34	36.66 ± 0.24	2199 ± 15	 	1500	57.09 ± 0.90	1.44 ± 0.21	39.77 ± 0.62		 	2000	9.2 ± 1.16	0.21 ± 0.14	44.73 ± 5.63		 	8.70 µM EncFtn-Enc	0	3.31 ± 1.57	6.85 ± 0.07	0.48 ± 0.23		 	224	116.27 ± 3.74	7.63 ± 0.12	15.25 ± 0.49		 	301	132.86 ± 4.03	6.66 ± 0.31	19.96 ± 0.61		 	450	220.57 ± 27.33	6.12 ± 1.07	36.06 ± 4.47		 	700	344.03 ± 40.38	6.94 ± 0.17	49.58 ± 5.82		 	1000	496.00 ± 38.48	7.19 ± 0.08	68.94 ± 5.35	4137 ± 321	 	1500	569.98 ± 73.63	5.73 ± 0.03	99.44 ± 12.84		 	2000	584.30 ± 28.33	4.88 ± 0.22	119.62 ± 5.80		 	8.50 µM Apoferritin	0	3.95 ± 2.26	9.37 ± 0.24	0.42 ± 0.25		 	42.5	10.27 ± 1.12	8.27 ± 0.30	1.24 ± 0.18		 	212.5	44.48 ± 2.76	7.85 ± 0.77	5.67 ± 0.83		 	637.5	160.93 ± 4.27	6.76 ± 0.81	23.79 ± 3.12	571 ± 75	 	1275	114.92 ± 3.17	3.84 ± 0.30	29.91 ± 2.95		 	1700	91.40 ± 3.37	3.14 ± 0.35	29.13 ± 3.86		 	"	TABLE
+125	127	Fe	chemical	"Protein sample	Fe(NH4)2(SO4)2 loading (µM)	Fe detected by ferrozine assay (µM)	Protein detected by BCA microplate assay (µM)	Fe / monomeric protein	Maximum Fe loading per biological assembly unit	 	8.46 µM EncFtnsH-10mer	0	4.73 ± 2.32	5.26 ± 0.64	0.90 ± 0.44		 	39.9	9.93 ± 1.20	5.36 ± 0.69	1.85 ± 0.22		 	84	17.99 ± 2.01	4.96 ± 0.04	3.63 ± 0.41		 	147	21.09 ± 1.94	4.44 ± 0.21	4.75 ± 0.44	48 ± 4	 	224	28.68 ± 0.30	3.73 ± 0.53	7.68 ± 0.08		 	301	11.27 ± 1.10	2.50 ± 0.05	4.51 ± 0.44		 	8.50 µM Encapsulin	0	-1.02 ± 0.54	8.63 ± 0.17	-0.12 ± 0.06		 	224	62.24 ± 2.49	10.01 ± 0.58	6.22 ± 0.35		 	301	67.94 ± 3.15	8.69 ± 0.42	7.81 ± 0.36		 	450	107.96 ± 8.88	8.50 ± 0.69	12.71 ± 1.05		 	700	97.51 ± 3.19	7.26 ± 0.20	13.44 ± 0.44		 	1000	308.63 ± 2.06	8.42 ± 0.34	36.66 ± 0.24	2199 ± 15	 	1500	57.09 ± 0.90	1.44 ± 0.21	39.77 ± 0.62		 	2000	9.2 ± 1.16	0.21 ± 0.14	44.73 ± 5.63		 	8.70 µM EncFtn-Enc	0	3.31 ± 1.57	6.85 ± 0.07	0.48 ± 0.23		 	224	116.27 ± 3.74	7.63 ± 0.12	15.25 ± 0.49		 	301	132.86 ± 4.03	6.66 ± 0.31	19.96 ± 0.61		 	450	220.57 ± 27.33	6.12 ± 1.07	36.06 ± 4.47		 	700	344.03 ± 40.38	6.94 ± 0.17	49.58 ± 5.82		 	1000	496.00 ± 38.48	7.19 ± 0.08	68.94 ± 5.35	4137 ± 321	 	1500	569.98 ± 73.63	5.73 ± 0.03	99.44 ± 12.84		 	2000	584.30 ± 28.33	4.88 ± 0.22	119.62 ± 5.80		 	8.50 µM Apoferritin	0	3.95 ± 2.26	9.37 ± 0.24	0.42 ± 0.25		 	42.5	10.27 ± 1.12	8.27 ± 0.30	1.24 ± 0.18		 	212.5	44.48 ± 2.76	7.85 ± 0.77	5.67 ± 0.83		 	637.5	160.93 ± 4.27	6.76 ± 0.81	23.79 ± 3.12	571 ± 75	 	1275	114.92 ± 3.17	3.84 ± 0.30	29.91 ± 2.95		 	1700	91.40 ± 3.37	3.14 ± 0.35	29.13 ± 3.86		 	"	TABLE
+156	158	Fe	chemical	"Protein sample	Fe(NH4)2(SO4)2 loading (µM)	Fe detected by ferrozine assay (µM)	Protein detected by BCA microplate assay (µM)	Fe / monomeric protein	Maximum Fe loading per biological assembly unit	 	8.46 µM EncFtnsH-10mer	0	4.73 ± 2.32	5.26 ± 0.64	0.90 ± 0.44		 	39.9	9.93 ± 1.20	5.36 ± 0.69	1.85 ± 0.22		 	84	17.99 ± 2.01	4.96 ± 0.04	3.63 ± 0.41		 	147	21.09 ± 1.94	4.44 ± 0.21	4.75 ± 0.44	48 ± 4	 	224	28.68 ± 0.30	3.73 ± 0.53	7.68 ± 0.08		 	301	11.27 ± 1.10	2.50 ± 0.05	4.51 ± 0.44		 	8.50 µM Encapsulin	0	-1.02 ± 0.54	8.63 ± 0.17	-0.12 ± 0.06		 	224	62.24 ± 2.49	10.01 ± 0.58	6.22 ± 0.35		 	301	67.94 ± 3.15	8.69 ± 0.42	7.81 ± 0.36		 	450	107.96 ± 8.88	8.50 ± 0.69	12.71 ± 1.05		 	700	97.51 ± 3.19	7.26 ± 0.20	13.44 ± 0.44		 	1000	308.63 ± 2.06	8.42 ± 0.34	36.66 ± 0.24	2199 ± 15	 	1500	57.09 ± 0.90	1.44 ± 0.21	39.77 ± 0.62		 	2000	9.2 ± 1.16	0.21 ± 0.14	44.73 ± 5.63		 	8.70 µM EncFtn-Enc	0	3.31 ± 1.57	6.85 ± 0.07	0.48 ± 0.23		 	224	116.27 ± 3.74	7.63 ± 0.12	15.25 ± 0.49		 	301	132.86 ± 4.03	6.66 ± 0.31	19.96 ± 0.61		 	450	220.57 ± 27.33	6.12 ± 1.07	36.06 ± 4.47		 	700	344.03 ± 40.38	6.94 ± 0.17	49.58 ± 5.82		 	1000	496.00 ± 38.48	7.19 ± 0.08	68.94 ± 5.35	4137 ± 321	 	1500	569.98 ± 73.63	5.73 ± 0.03	99.44 ± 12.84		 	2000	584.30 ± 28.33	4.88 ± 0.22	119.62 ± 5.80		 	8.50 µM Apoferritin	0	3.95 ± 2.26	9.37 ± 0.24	0.42 ± 0.25		 	42.5	10.27 ± 1.12	8.27 ± 0.30	1.24 ± 0.18		 	212.5	44.48 ± 2.76	7.85 ± 0.77	5.67 ± 0.83		 	637.5	160.93 ± 4.27	6.76 ± 0.81	23.79 ± 3.12	571 ± 75	 	1275	114.92 ± 3.17	3.84 ± 0.30	29.91 ± 2.95		 	1700	91.40 ± 3.37	3.14 ± 0.35	29.13 ± 3.86		 	"	TABLE
+206	214	EncFtnsH	protein	"Protein sample	Fe(NH4)2(SO4)2 loading (µM)	Fe detected by ferrozine assay (µM)	Protein detected by BCA microplate assay (µM)	Fe / monomeric protein	Maximum Fe loading per biological assembly unit	 	8.46 µM EncFtnsH-10mer	0	4.73 ± 2.32	5.26 ± 0.64	0.90 ± 0.44		 	39.9	9.93 ± 1.20	5.36 ± 0.69	1.85 ± 0.22		 	84	17.99 ± 2.01	4.96 ± 0.04	3.63 ± 0.41		 	147	21.09 ± 1.94	4.44 ± 0.21	4.75 ± 0.44	48 ± 4	 	224	28.68 ± 0.30	3.73 ± 0.53	7.68 ± 0.08		 	301	11.27 ± 1.10	2.50 ± 0.05	4.51 ± 0.44		 	8.50 µM Encapsulin	0	-1.02 ± 0.54	8.63 ± 0.17	-0.12 ± 0.06		 	224	62.24 ± 2.49	10.01 ± 0.58	6.22 ± 0.35		 	301	67.94 ± 3.15	8.69 ± 0.42	7.81 ± 0.36		 	450	107.96 ± 8.88	8.50 ± 0.69	12.71 ± 1.05		 	700	97.51 ± 3.19	7.26 ± 0.20	13.44 ± 0.44		 	1000	308.63 ± 2.06	8.42 ± 0.34	36.66 ± 0.24	2199 ± 15	 	1500	57.09 ± 0.90	1.44 ± 0.21	39.77 ± 0.62		 	2000	9.2 ± 1.16	0.21 ± 0.14	44.73 ± 5.63		 	8.70 µM EncFtn-Enc	0	3.31 ± 1.57	6.85 ± 0.07	0.48 ± 0.23		 	224	116.27 ± 3.74	7.63 ± 0.12	15.25 ± 0.49		 	301	132.86 ± 4.03	6.66 ± 0.31	19.96 ± 0.61		 	450	220.57 ± 27.33	6.12 ± 1.07	36.06 ± 4.47		 	700	344.03 ± 40.38	6.94 ± 0.17	49.58 ± 5.82		 	1000	496.00 ± 38.48	7.19 ± 0.08	68.94 ± 5.35	4137 ± 321	 	1500	569.98 ± 73.63	5.73 ± 0.03	99.44 ± 12.84		 	2000	584.30 ± 28.33	4.88 ± 0.22	119.62 ± 5.80		 	8.50 µM Apoferritin	0	3.95 ± 2.26	9.37 ± 0.24	0.42 ± 0.25		 	42.5	10.27 ± 1.12	8.27 ± 0.30	1.24 ± 0.18		 	212.5	44.48 ± 2.76	7.85 ± 0.77	5.67 ± 0.83		 	637.5	160.93 ± 4.27	6.76 ± 0.81	23.79 ± 3.12	571 ± 75	 	1275	114.92 ± 3.17	3.84 ± 0.30	29.91 ± 2.95		 	1700	91.40 ± 3.37	3.14 ± 0.35	29.13 ± 3.86		 	"	TABLE
+215	220	10mer	oligomeric_state	"Protein sample	Fe(NH4)2(SO4)2 loading (µM)	Fe detected by ferrozine assay (µM)	Protein detected by BCA microplate assay (µM)	Fe / monomeric protein	Maximum Fe loading per biological assembly unit	 	8.46 µM EncFtnsH-10mer	0	4.73 ± 2.32	5.26 ± 0.64	0.90 ± 0.44		 	39.9	9.93 ± 1.20	5.36 ± 0.69	1.85 ± 0.22		 	84	17.99 ± 2.01	4.96 ± 0.04	3.63 ± 0.41		 	147	21.09 ± 1.94	4.44 ± 0.21	4.75 ± 0.44	48 ± 4	 	224	28.68 ± 0.30	3.73 ± 0.53	7.68 ± 0.08		 	301	11.27 ± 1.10	2.50 ± 0.05	4.51 ± 0.44		 	8.50 µM Encapsulin	0	-1.02 ± 0.54	8.63 ± 0.17	-0.12 ± 0.06		 	224	62.24 ± 2.49	10.01 ± 0.58	6.22 ± 0.35		 	301	67.94 ± 3.15	8.69 ± 0.42	7.81 ± 0.36		 	450	107.96 ± 8.88	8.50 ± 0.69	12.71 ± 1.05		 	700	97.51 ± 3.19	7.26 ± 0.20	13.44 ± 0.44		 	1000	308.63 ± 2.06	8.42 ± 0.34	36.66 ± 0.24	2199 ± 15	 	1500	57.09 ± 0.90	1.44 ± 0.21	39.77 ± 0.62		 	2000	9.2 ± 1.16	0.21 ± 0.14	44.73 ± 5.63		 	8.70 µM EncFtn-Enc	0	3.31 ± 1.57	6.85 ± 0.07	0.48 ± 0.23		 	224	116.27 ± 3.74	7.63 ± 0.12	15.25 ± 0.49		 	301	132.86 ± 4.03	6.66 ± 0.31	19.96 ± 0.61		 	450	220.57 ± 27.33	6.12 ± 1.07	36.06 ± 4.47		 	700	344.03 ± 40.38	6.94 ± 0.17	49.58 ± 5.82		 	1000	496.00 ± 38.48	7.19 ± 0.08	68.94 ± 5.35	4137 ± 321	 	1500	569.98 ± 73.63	5.73 ± 0.03	99.44 ± 12.84		 	2000	584.30 ± 28.33	4.88 ± 0.22	119.62 ± 5.80		 	8.50 µM Apoferritin	0	3.95 ± 2.26	9.37 ± 0.24	0.42 ± 0.25		 	42.5	10.27 ± 1.12	8.27 ± 0.30	1.24 ± 0.18		 	212.5	44.48 ± 2.76	7.85 ± 0.77	5.67 ± 0.83		 	637.5	160.93 ± 4.27	6.76 ± 0.81	23.79 ± 3.12	571 ± 75	 	1275	114.92 ± 3.17	3.84 ± 0.30	29.91 ± 2.95		 	1700	91.40 ± 3.37	3.14 ± 0.35	29.13 ± 3.86		 	"	TABLE
+495	505	Encapsulin	protein	"Protein sample	Fe(NH4)2(SO4)2 loading (µM)	Fe detected by ferrozine assay (µM)	Protein detected by BCA microplate assay (µM)	Fe / monomeric protein	Maximum Fe loading per biological assembly unit	 	8.46 µM EncFtnsH-10mer	0	4.73 ± 2.32	5.26 ± 0.64	0.90 ± 0.44		 	39.9	9.93 ± 1.20	5.36 ± 0.69	1.85 ± 0.22		 	84	17.99 ± 2.01	4.96 ± 0.04	3.63 ± 0.41		 	147	21.09 ± 1.94	4.44 ± 0.21	4.75 ± 0.44	48 ± 4	 	224	28.68 ± 0.30	3.73 ± 0.53	7.68 ± 0.08		 	301	11.27 ± 1.10	2.50 ± 0.05	4.51 ± 0.44		 	8.50 µM Encapsulin	0	-1.02 ± 0.54	8.63 ± 0.17	-0.12 ± 0.06		 	224	62.24 ± 2.49	10.01 ± 0.58	6.22 ± 0.35		 	301	67.94 ± 3.15	8.69 ± 0.42	7.81 ± 0.36		 	450	107.96 ± 8.88	8.50 ± 0.69	12.71 ± 1.05		 	700	97.51 ± 3.19	7.26 ± 0.20	13.44 ± 0.44		 	1000	308.63 ± 2.06	8.42 ± 0.34	36.66 ± 0.24	2199 ± 15	 	1500	57.09 ± 0.90	1.44 ± 0.21	39.77 ± 0.62		 	2000	9.2 ± 1.16	0.21 ± 0.14	44.73 ± 5.63		 	8.70 µM EncFtn-Enc	0	3.31 ± 1.57	6.85 ± 0.07	0.48 ± 0.23		 	224	116.27 ± 3.74	7.63 ± 0.12	15.25 ± 0.49		 	301	132.86 ± 4.03	6.66 ± 0.31	19.96 ± 0.61		 	450	220.57 ± 27.33	6.12 ± 1.07	36.06 ± 4.47		 	700	344.03 ± 40.38	6.94 ± 0.17	49.58 ± 5.82		 	1000	496.00 ± 38.48	7.19 ± 0.08	68.94 ± 5.35	4137 ± 321	 	1500	569.98 ± 73.63	5.73 ± 0.03	99.44 ± 12.84		 	2000	584.30 ± 28.33	4.88 ± 0.22	119.62 ± 5.80		 	8.50 µM Apoferritin	0	3.95 ± 2.26	9.37 ± 0.24	0.42 ± 0.25		 	42.5	10.27 ± 1.12	8.27 ± 0.30	1.24 ± 0.18		 	212.5	44.48 ± 2.76	7.85 ± 0.77	5.67 ± 0.83		 	637.5	160.93 ± 4.27	6.76 ± 0.81	23.79 ± 3.12	571 ± 75	 	1275	114.92 ± 3.17	3.84 ± 0.30	29.91 ± 2.95		 	1700	91.40 ± 3.37	3.14 ± 0.35	29.13 ± 3.86		 	"	TABLE
+883	893	EncFtn-Enc	complex_assembly	"Protein sample	Fe(NH4)2(SO4)2 loading (µM)	Fe detected by ferrozine assay (µM)	Protein detected by BCA microplate assay (µM)	Fe / monomeric protein	Maximum Fe loading per biological assembly unit	 	8.46 µM EncFtnsH-10mer	0	4.73 ± 2.32	5.26 ± 0.64	0.90 ± 0.44		 	39.9	9.93 ± 1.20	5.36 ± 0.69	1.85 ± 0.22		 	84	17.99 ± 2.01	4.96 ± 0.04	3.63 ± 0.41		 	147	21.09 ± 1.94	4.44 ± 0.21	4.75 ± 0.44	48 ± 4	 	224	28.68 ± 0.30	3.73 ± 0.53	7.68 ± 0.08		 	301	11.27 ± 1.10	2.50 ± 0.05	4.51 ± 0.44		 	8.50 µM Encapsulin	0	-1.02 ± 0.54	8.63 ± 0.17	-0.12 ± 0.06		 	224	62.24 ± 2.49	10.01 ± 0.58	6.22 ± 0.35		 	301	67.94 ± 3.15	8.69 ± 0.42	7.81 ± 0.36		 	450	107.96 ± 8.88	8.50 ± 0.69	12.71 ± 1.05		 	700	97.51 ± 3.19	7.26 ± 0.20	13.44 ± 0.44		 	1000	308.63 ± 2.06	8.42 ± 0.34	36.66 ± 0.24	2199 ± 15	 	1500	57.09 ± 0.90	1.44 ± 0.21	39.77 ± 0.62		 	2000	9.2 ± 1.16	0.21 ± 0.14	44.73 ± 5.63		 	8.70 µM EncFtn-Enc	0	3.31 ± 1.57	6.85 ± 0.07	0.48 ± 0.23		 	224	116.27 ± 3.74	7.63 ± 0.12	15.25 ± 0.49		 	301	132.86 ± 4.03	6.66 ± 0.31	19.96 ± 0.61		 	450	220.57 ± 27.33	6.12 ± 1.07	36.06 ± 4.47		 	700	344.03 ± 40.38	6.94 ± 0.17	49.58 ± 5.82		 	1000	496.00 ± 38.48	7.19 ± 0.08	68.94 ± 5.35	4137 ± 321	 	1500	569.98 ± 73.63	5.73 ± 0.03	99.44 ± 12.84		 	2000	584.30 ± 28.33	4.88 ± 0.22	119.62 ± 5.80		 	8.50 µM Apoferritin	0	3.95 ± 2.26	9.37 ± 0.24	0.42 ± 0.25		 	42.5	10.27 ± 1.12	8.27 ± 0.30	1.24 ± 0.18		 	212.5	44.48 ± 2.76	7.85 ± 0.77	5.67 ± 0.83		 	637.5	160.93 ± 4.27	6.76 ± 0.81	23.79 ± 3.12	571 ± 75	 	1275	114.92 ± 3.17	3.84 ± 0.30	29.91 ± 2.95		 	1700	91.40 ± 3.37	3.14 ± 0.35	29.13 ± 3.86		 	"	TABLE
+1285	1296	Apoferritin	protein_state	"Protein sample	Fe(NH4)2(SO4)2 loading (µM)	Fe detected by ferrozine assay (µM)	Protein detected by BCA microplate assay (µM)	Fe / monomeric protein	Maximum Fe loading per biological assembly unit	 	8.46 µM EncFtnsH-10mer	0	4.73 ± 2.32	5.26 ± 0.64	0.90 ± 0.44		 	39.9	9.93 ± 1.20	5.36 ± 0.69	1.85 ± 0.22		 	84	17.99 ± 2.01	4.96 ± 0.04	3.63 ± 0.41		 	147	21.09 ± 1.94	4.44 ± 0.21	4.75 ± 0.44	48 ± 4	 	224	28.68 ± 0.30	3.73 ± 0.53	7.68 ± 0.08		 	301	11.27 ± 1.10	2.50 ± 0.05	4.51 ± 0.44		 	8.50 µM Encapsulin	0	-1.02 ± 0.54	8.63 ± 0.17	-0.12 ± 0.06		 	224	62.24 ± 2.49	10.01 ± 0.58	6.22 ± 0.35		 	301	67.94 ± 3.15	8.69 ± 0.42	7.81 ± 0.36		 	450	107.96 ± 8.88	8.50 ± 0.69	12.71 ± 1.05		 	700	97.51 ± 3.19	7.26 ± 0.20	13.44 ± 0.44		 	1000	308.63 ± 2.06	8.42 ± 0.34	36.66 ± 0.24	2199 ± 15	 	1500	57.09 ± 0.90	1.44 ± 0.21	39.77 ± 0.62		 	2000	9.2 ± 1.16	0.21 ± 0.14	44.73 ± 5.63		 	8.70 µM EncFtn-Enc	0	3.31 ± 1.57	6.85 ± 0.07	0.48 ± 0.23		 	224	116.27 ± 3.74	7.63 ± 0.12	15.25 ± 0.49		 	301	132.86 ± 4.03	6.66 ± 0.31	19.96 ± 0.61		 	450	220.57 ± 27.33	6.12 ± 1.07	36.06 ± 4.47		 	700	344.03 ± 40.38	6.94 ± 0.17	49.58 ± 5.82		 	1000	496.00 ± 38.48	7.19 ± 0.08	68.94 ± 5.35	4137 ± 321	 	1500	569.98 ± 73.63	5.73 ± 0.03	99.44 ± 12.84		 	2000	584.30 ± 28.33	4.88 ± 0.22	119.62 ± 5.80		 	8.50 µM Apoferritin	0	3.95 ± 2.26	9.37 ± 0.24	0.42 ± 0.25		 	42.5	10.27 ± 1.12	8.27 ± 0.30	1.24 ± 0.18		 	212.5	44.48 ± 2.76	7.85 ± 0.77	5.67 ± 0.83		 	637.5	160.93 ± 4.27	6.76 ± 0.81	23.79 ± 3.12	571 ± 75	 	1275	114.92 ± 3.17	3.84 ± 0.30	29.91 ± 2.95		 	1700	91.40 ± 3.37	3.14 ± 0.35	29.13 ± 3.86		 	"	TABLE
+32	39	mutants	protein_state	To understand the impact of the mutants on the organization and metal binding of the FOC, we determined the X-ray crystal structures of each of the EncFtnsH mutants (See Table 4 for data collection and refinement statistics).	RESULTS
+85	88	FOC	site	To understand the impact of the mutants on the organization and metal binding of the FOC, we determined the X-ray crystal structures of each of the EncFtnsH mutants (See Table 4 for data collection and refinement statistics).	RESULTS
+108	132	X-ray crystal structures	evidence	To understand the impact of the mutants on the organization and metal binding of the FOC, we determined the X-ray crystal structures of each of the EncFtnsH mutants (See Table 4 for data collection and refinement statistics).	RESULTS
+148	156	EncFtnsH	protein	To understand the impact of the mutants on the organization and metal binding of the FOC, we determined the X-ray crystal structures of each of the EncFtnsH mutants (See Table 4 for data collection and refinement statistics).	RESULTS
+157	164	mutants	protein_state	To understand the impact of the mutants on the organization and metal binding of the FOC, we determined the X-ray crystal structures of each of the EncFtnsH mutants (See Table 4 for data collection and refinement statistics).	RESULTS
+34	41	mutants	protein_state	The crystal packing of all of the mutants in this study is essentially isomorphous to the EncFtnsH structure.	RESULTS
+90	98	EncFtnsH	protein	The crystal packing of all of the mutants in this study is essentially isomorphous to the EncFtnsH structure.	RESULTS
+99	108	structure	evidence	The crystal packing of all of the mutants in this study is essentially isomorphous to the EncFtnsH structure.	RESULTS
+11	18	mutants	protein_state	All of the mutants display the same decameric arrangement in the crystals as the EncFtnsH structure, and the monomers superimpose with an average RMSDCα of less than 0.2 Å.	RESULTS
+36	45	decameric	oligomeric_state	All of the mutants display the same decameric arrangement in the crystals as the EncFtnsH structure, and the monomers superimpose with an average RMSDCα of less than 0.2 Å.	RESULTS
+65	73	crystals	evidence	All of the mutants display the same decameric arrangement in the crystals as the EncFtnsH structure, and the monomers superimpose with an average RMSDCα of less than 0.2 Å.	RESULTS
+81	89	EncFtnsH	protein	All of the mutants display the same decameric arrangement in the crystals as the EncFtnsH structure, and the monomers superimpose with an average RMSDCα of less than 0.2 Å.	RESULTS
+90	99	structure	evidence	All of the mutants display the same decameric arrangement in the crystals as the EncFtnsH structure, and the monomers superimpose with an average RMSDCα of less than 0.2 Å.	RESULTS
+109	117	monomers	oligomeric_state	All of the mutants display the same decameric arrangement in the crystals as the EncFtnsH structure, and the monomers superimpose with an average RMSDCα of less than 0.2 Å.	RESULTS
+118	129	superimpose	experimental_method	All of the mutants display the same decameric arrangement in the crystals as the EncFtnsH structure, and the monomers superimpose with an average RMSDCα of less than 0.2 Å.	RESULTS
+146	152	RMSDCα	evidence	All of the mutants display the same decameric arrangement in the crystals as the EncFtnsH structure, and the monomers superimpose with an average RMSDCα of less than 0.2 Å.	RESULTS
+0	3	FOC	site	FOC dimer interface of EncFtnsH-E32A mutant.	FIG
+4	19	dimer interface	site	FOC dimer interface of EncFtnsH-E32A mutant.	FIG
+23	36	EncFtnsH-E32A	mutant	FOC dimer interface of EncFtnsH-E32A mutant.	FIG
+37	43	mutant	protein_state	FOC dimer interface of EncFtnsH-E32A mutant.	FIG
+33	69	metal-binding dimerization interface	site	(A) Wall-eyed stereo view of the metal-binding dimerization interface of EncFtnsH-E32A.	FIG
+73	86	EncFtnsH-E32A	mutant	(A) Wall-eyed stereo view of the metal-binding dimerization interface of EncFtnsH-E32A.	FIG
+83	91	subunits	structure_element	Protein residues are shown as sticks with blue and green carbons for the different subunits.	FIG
+83	91	subunits	structure_element	Protein residues are shown as sticks with blue and green carbons for the different subunits.	FIG
+83	91	subunits	structure_element	Protein residues are shown as sticks with blue and green carbons for the different subunits.	FIG
+4	33	2mFo-DFc electron density map	evidence	The 2mFo-DFc electron density map is shown as a blue mesh contoured at 1.5 σ.	FIG
+4	33	2mFo-DFc electron density map	evidence	The 2mFo-DFc electron density map is shown as a blue mesh contoured at 1.5 σ.	FIG
+4	33	2mFo-DFc electron density map	evidence	The 2mFo-DFc electron density map is shown as a blue mesh contoured at 1.5 σ.	FIG
+17	20	FOC	site	(B) Views of the FOC of the EncFtnsH-E32Amutant.	FIG
+28	41	EncFtnsH-E32A	mutant	(B) Views of the FOC of the EncFtnsH-E32Amutant.	FIG
+41	47	mutant	protein_state	(B) Views of the FOC of the EncFtnsH-E32Amutant.	FIG
+0	19	FOC dimer interface	site	FOC dimer interface of EncFtnsH-E62A mutant.	FIG
+23	36	EncFtnsH-E62A	mutant	FOC dimer interface of EncFtnsH-E62A mutant.	FIG
+37	43	mutant	protein_state	FOC dimer interface of EncFtnsH-E62A mutant.	FIG
+33	69	metal-binding dimerization interface	site	(A) Wall-eyed stereo view of the metal-binding dimerization interface of EncFtnsH-E62A.	FIG
+73	86	EncFtnsH-E62A	mutant	(A) Wall-eyed stereo view of the metal-binding dimerization interface of EncFtnsH-E62A.	FIG
+23	30	calcium	chemical	The single coordinated calcium ion is shown as a grey sphere. (B) Views of the FOC of the EncFtnsH-E62A mutant.	FIG
+79	82	FOC	site	The single coordinated calcium ion is shown as a grey sphere. (B) Views of the FOC of the EncFtnsH-E62A mutant.	FIG
+90	103	EncFtnsH-E62A	mutant	The single coordinated calcium ion is shown as a grey sphere. (B) Views of the FOC of the EncFtnsH-E62A mutant.	FIG
+104	110	mutant	protein_state	The single coordinated calcium ion is shown as a grey sphere. (B) Views of the FOC of the EncFtnsH-E62A mutant.	FIG
+0	19	FOC dimer interface	site	FOC dimer interface of EncFtnsH-H65A mutant.	FIG
+23	36	EncFtnsH-H65A	mutant	FOC dimer interface of EncFtnsH-H65A mutant.	FIG
+37	43	mutant	protein_state	FOC dimer interface of EncFtnsH-H65A mutant.	FIG
+33	69	metal-binding dimerization interface	site	(A) Wall-eyed stereo view of the metal-binding dimerization interface of EncFtnsH-H65A.	FIG
+73	86	EncFtnsH-H65A	mutant	(A) Wall-eyed stereo view of the metal-binding dimerization interface of EncFtnsH-H65A.	FIG
+16	23	calcium	chemical	The coordinated calcium ions are shown as a grey spheres with coordination distances in the FOC highlighted with yellow dashed lines.	FIG
+62	74	coordination	bond_interaction	The coordinated calcium ions are shown as a grey spheres with coordination distances in the FOC highlighted with yellow dashed lines.	FIG
+92	95	FOC	site	The coordinated calcium ions are shown as a grey spheres with coordination distances in the FOC highlighted with yellow dashed lines.	FIG
+17	20	FOC	site	(B) Views of the FOC of the EncFtnsH-H65A mutant.	FIG
+28	41	EncFtnsH-H65A	mutant	(B) Views of the FOC of the EncFtnsH-H65A mutant.	FIG
+42	48	mutant	protein_state	(B) Views of the FOC of the EncFtnsH-H65A mutant.	FIG
+18	26	EncFtnsH	protein	Comparison of the EncFtnsH FOC mutants vs wild type.	FIG
+27	30	FOC	site	Comparison of the EncFtnsH FOC mutants vs wild type.	FIG
+31	38	mutants	protein_state	Comparison of the EncFtnsH FOC mutants vs wild type.	FIG
+42	51	wild type	protein_state	Comparison of the EncFtnsH FOC mutants vs wild type.	FIG
+4	14	structures	evidence	The structures of the three EncFtnsH mutants were all determined by X-ray crystallography.	FIG
+28	36	EncFtnsH	protein	The structures of the three EncFtnsH mutants were all determined by X-ray crystallography.	FIG
+37	44	mutants	protein_state	The structures of the three EncFtnsH mutants were all determined by X-ray crystallography.	FIG
+68	89	X-ray crystallography	experimental_method	The structures of the three EncFtnsH mutants were all determined by X-ray crystallography.	FIG
+4	8	E32A	mutant	The E32A, E62A and H65A mutants were crystallized in identical conditions to the wild type.	FIG
+10	14	E62A	mutant	The E32A, E62A and H65A mutants were crystallized in identical conditions to the wild type.	FIG
+19	23	H65A	mutant	The E32A, E62A and H65A mutants were crystallized in identical conditions to the wild type.	FIG
+24	31	mutants	protein_state	The E32A, E62A and H65A mutants were crystallized in identical conditions to the wild type.	FIG
+37	49	crystallized	experimental_method	The E32A, E62A and H65A mutants were crystallized in identical conditions to the wild type.	FIG
+81	90	wild type	protein_state	The E32A, E62A and H65A mutants were crystallized in identical conditions to the wild type.	FIG
+0	8	EncFtnsH	protein	EncFtnsH structure and were essentially isomorphous in terms of their unit cell dimensions.	FIG
+9	18	structure	evidence	EncFtnsH structure and were essentially isomorphous in terms of their unit cell dimensions.	FIG
+4	7	FOC	site	The FOC residues of the mutants and native EncFtnsH structures are shown as sticks with coordinated Fe2+ as orange and Ca2+ as grey spheres and are colored as follows: wild type, grey; E32A, pink; E62A, green; H65A, blue.	FIG
+24	31	mutants	protein_state	The FOC residues of the mutants and native EncFtnsH structures are shown as sticks with coordinated Fe2+ as orange and Ca2+ as grey spheres and are colored as follows: wild type, grey; E32A, pink; E62A, green; H65A, blue.	FIG
+36	42	native	protein_state	The FOC residues of the mutants and native EncFtnsH structures are shown as sticks with coordinated Fe2+ as orange and Ca2+ as grey spheres and are colored as follows: wild type, grey; E32A, pink; E62A, green; H65A, blue.	FIG
+43	51	EncFtnsH	protein	The FOC residues of the mutants and native EncFtnsH structures are shown as sticks with coordinated Fe2+ as orange and Ca2+ as grey spheres and are colored as follows: wild type, grey; E32A, pink; E62A, green; H65A, blue.	FIG
+52	62	structures	evidence	The FOC residues of the mutants and native EncFtnsH structures are shown as sticks with coordinated Fe2+ as orange and Ca2+ as grey spheres and are colored as follows: wild type, grey; E32A, pink; E62A, green; H65A, blue.	FIG
+88	99	coordinated	bond_interaction	The FOC residues of the mutants and native EncFtnsH structures are shown as sticks with coordinated Fe2+ as orange and Ca2+ as grey spheres and are colored as follows: wild type, grey; E32A, pink; E62A, green; H65A, blue.	FIG
+100	104	Fe2+	chemical	The FOC residues of the mutants and native EncFtnsH structures are shown as sticks with coordinated Fe2+ as orange and Ca2+ as grey spheres and are colored as follows: wild type, grey; E32A, pink; E62A, green; H65A, blue.	FIG
+119	123	Ca2+	chemical	The FOC residues of the mutants and native EncFtnsH structures are shown as sticks with coordinated Fe2+ as orange and Ca2+ as grey spheres and are colored as follows: wild type, grey; E32A, pink; E62A, green; H65A, blue.	FIG
+168	177	wild type	protein_state	The FOC residues of the mutants and native EncFtnsH structures are shown as sticks with coordinated Fe2+ as orange and Ca2+ as grey spheres and are colored as follows: wild type, grey; E32A, pink; E62A, green; H65A, blue.	FIG
+185	189	E32A	mutant	The FOC residues of the mutants and native EncFtnsH structures are shown as sticks with coordinated Fe2+ as orange and Ca2+ as grey spheres and are colored as follows: wild type, grey; E32A, pink; E62A, green; H65A, blue.	FIG
+197	201	E62A	mutant	The FOC residues of the mutants and native EncFtnsH structures are shown as sticks with coordinated Fe2+ as orange and Ca2+ as grey spheres and are colored as follows: wild type, grey; E32A, pink; E62A, green; H65A, blue.	FIG
+210	214	H65A	mutant	The FOC residues of the mutants and native EncFtnsH structures are shown as sticks with coordinated Fe2+ as orange and Ca2+ as grey spheres and are colored as follows: wild type, grey; E32A, pink; E62A, green; H65A, blue.	FIG
+7	14	mutants	protein_state	Of the mutants, only H65A has any coordinated metal ions, which appear to be calcium ions from the crystallization condition.	FIG
+21	25	H65A	mutant	Of the mutants, only H65A has any coordinated metal ions, which appear to be calcium ions from the crystallization condition.	FIG
+34	45	coordinated	bond_interaction	Of the mutants, only H65A has any coordinated metal ions, which appear to be calcium ions from the crystallization condition.	FIG
+77	84	calcium	chemical	Of the mutants, only H65A has any coordinated metal ions, which appear to be calcium ions from the crystallization condition.	FIG
+28	31	FOC	site	The overall organization of FOC residues is retained in the mutants, with almost no backbone movements.	FIG
+60	67	mutants	protein_state	The overall organization of FOC residues is retained in the mutants, with almost no backbone movements.	FIG
+38	43	Tyr39	residue_name_number	Significant differences center around Tyr39, which moves to coordinate the bound calcium ions in the H65A mutant; and Glu32, which moves away from the metal ions in this structure.	FIG
+60	70	coordinate	bond_interaction	Significant differences center around Tyr39, which moves to coordinate the bound calcium ions in the H65A mutant; and Glu32, which moves away from the metal ions in this structure.	FIG
+75	80	bound	protein_state	Significant differences center around Tyr39, which moves to coordinate the bound calcium ions in the H65A mutant; and Glu32, which moves away from the metal ions in this structure.	FIG
+81	88	calcium	chemical	Significant differences center around Tyr39, which moves to coordinate the bound calcium ions in the H65A mutant; and Glu32, which moves away from the metal ions in this structure.	FIG
+101	105	H65A	mutant	Significant differences center around Tyr39, which moves to coordinate the bound calcium ions in the H65A mutant; and Glu32, which moves away from the metal ions in this structure.	FIG
+106	112	mutant	protein_state	Significant differences center around Tyr39, which moves to coordinate the bound calcium ions in the H65A mutant; and Glu32, which moves away from the metal ions in this structure.	FIG
+118	123	Glu32	residue_name_number	Significant differences center around Tyr39, which moves to coordinate the bound calcium ions in the H65A mutant; and Glu32, which moves away from the metal ions in this structure.	FIG
+170	179	structure	evidence	Significant differences center around Tyr39, which moves to coordinate the bound calcium ions in the H65A mutant; and Glu32, which moves away from the metal ions in this structure.	FIG
+57	60	FOC	site	Close inspection of the region of the protein around the FOC in each of the mutants highlights their effect on metal binding (Figure 11 and Figure 11—figure supplement 1–3).	RESULTS
+76	83	mutants	protein_state	Close inspection of the region of the protein around the FOC in each of the mutants highlights their effect on metal binding (Figure 11 and Figure 11—figure supplement 1–3).	RESULTS
+7	11	E32A	mutant	In the E32A mutant the position of the side chains of the remaining iron coordinating residues in the FOC is essentially unchanged, but the absence of the axial-metal coordinating ligand provided by the Glu32 side chain abrogates metal binding in this site.	RESULTS
+12	18	mutant	protein_state	In the E32A mutant the position of the side chains of the remaining iron coordinating residues in the FOC is essentially unchanged, but the absence of the axial-metal coordinating ligand provided by the Glu32 side chain abrogates metal binding in this site.	RESULTS
+68	94	iron coordinating residues	site	In the E32A mutant the position of the side chains of the remaining iron coordinating residues in the FOC is essentially unchanged, but the absence of the axial-metal coordinating ligand provided by the Glu32 side chain abrogates metal binding in this site.	RESULTS
+102	105	FOC	site	In the E32A mutant the position of the side chains of the remaining iron coordinating residues in the FOC is essentially unchanged, but the absence of the axial-metal coordinating ligand provided by the Glu32 side chain abrogates metal binding in this site.	RESULTS
+140	150	absence of	protein_state	In the E32A mutant the position of the side chains of the remaining iron coordinating residues in the FOC is essentially unchanged, but the absence of the axial-metal coordinating ligand provided by the Glu32 side chain abrogates metal binding in this site.	RESULTS
+167	179	coordinating	bond_interaction	In the E32A mutant the position of the side chains of the remaining iron coordinating residues in the FOC is essentially unchanged, but the absence of the axial-metal coordinating ligand provided by the Glu32 side chain abrogates metal binding in this site.	RESULTS
+203	208	Glu32	residue_name_number	In the E32A mutant the position of the side chains of the remaining iron coordinating residues in the FOC is essentially unchanged, but the absence of the axial-metal coordinating ligand provided by the Glu32 side chain abrogates metal binding in this site.	RESULTS
+220	243	abrogates metal binding	protein_state	In the E32A mutant the position of the side chains of the remaining iron coordinating residues in the FOC is essentially unchanged, but the absence of the axial-metal coordinating ligand provided by the Glu32 side chain abrogates metal binding in this site.	RESULTS
+4	17	Glu31/34-site	site	The Glu31/34-site also lacks metal, with the side chain of Glu31 rotated by 180° at the Cβ in the absence of metal (Figure 11—figure supplement 1).	RESULTS
+23	28	lacks	protein_state	The Glu31/34-site also lacks metal, with the side chain of Glu31 rotated by 180° at the Cβ in the absence of metal (Figure 11—figure supplement 1).	RESULTS
+29	34	metal	chemical	The Glu31/34-site also lacks metal, with the side chain of Glu31 rotated by 180° at the Cβ in the absence of metal (Figure 11—figure supplement 1).	RESULTS
+59	64	Glu31	residue_name_number	The Glu31/34-site also lacks metal, with the side chain of Glu31 rotated by 180° at the Cβ in the absence of metal (Figure 11—figure supplement 1).	RESULTS
+98	108	absence of	protein_state	The Glu31/34-site also lacks metal, with the side chain of Glu31 rotated by 180° at the Cβ in the absence of metal (Figure 11—figure supplement 1).	RESULTS
+109	114	metal	chemical	The Glu31/34-site also lacks metal, with the side chain of Glu31 rotated by 180° at the Cβ in the absence of metal (Figure 11—figure supplement 1).	RESULTS
+4	8	E62A	mutant	The E62A mutant has a similar effect on the FOC to the E32A mutant, however the entry site still has a calcium ion coordinated between residues Glu31 and Glu34 (Figure 11—figure supplement 2).	RESULTS
+9	15	mutant	protein_state	The E62A mutant has a similar effect on the FOC to the E32A mutant, however the entry site still has a calcium ion coordinated between residues Glu31 and Glu34 (Figure 11—figure supplement 2).	RESULTS
+44	47	FOC	site	The E62A mutant has a similar effect on the FOC to the E32A mutant, however the entry site still has a calcium ion coordinated between residues Glu31 and Glu34 (Figure 11—figure supplement 2).	RESULTS
+55	59	E32A	mutant	The E62A mutant has a similar effect on the FOC to the E32A mutant, however the entry site still has a calcium ion coordinated between residues Glu31 and Glu34 (Figure 11—figure supplement 2).	RESULTS
+60	66	mutant	protein_state	The E62A mutant has a similar effect on the FOC to the E32A mutant, however the entry site still has a calcium ion coordinated between residues Glu31 and Glu34 (Figure 11—figure supplement 2).	RESULTS
+80	90	entry site	site	The E62A mutant has a similar effect on the FOC to the E32A mutant, however the entry site still has a calcium ion coordinated between residues Glu31 and Glu34 (Figure 11—figure supplement 2).	RESULTS
+103	110	calcium	chemical	The E62A mutant has a similar effect on the FOC to the E32A mutant, however the entry site still has a calcium ion coordinated between residues Glu31 and Glu34 (Figure 11—figure supplement 2).	RESULTS
+115	126	coordinated	bond_interaction	The E62A mutant has a similar effect on the FOC to the E32A mutant, however the entry site still has a calcium ion coordinated between residues Glu31 and Glu34 (Figure 11—figure supplement 2).	RESULTS
+144	149	Glu31	residue_name_number	The E62A mutant has a similar effect on the FOC to the E32A mutant, however the entry site still has a calcium ion coordinated between residues Glu31 and Glu34 (Figure 11—figure supplement 2).	RESULTS
+154	159	Glu34	residue_name_number	The E62A mutant has a similar effect on the FOC to the E32A mutant, however the entry site still has a calcium ion coordinated between residues Glu31 and Glu34 (Figure 11—figure supplement 2).	RESULTS
+4	8	H65A	mutant	The H65A mutant diverges significantly from the wild type in the position of the residues Glu32 and Tyr39 in the FOC.	RESULTS
+9	15	mutant	protein_state	The H65A mutant diverges significantly from the wild type in the position of the residues Glu32 and Tyr39 in the FOC.	RESULTS
+48	57	wild type	protein_state	The H65A mutant diverges significantly from the wild type in the position of the residues Glu32 and Tyr39 in the FOC.	RESULTS
+90	95	Glu32	residue_name_number	The H65A mutant diverges significantly from the wild type in the position of the residues Glu32 and Tyr39 in the FOC.	RESULTS
+100	105	Tyr39	residue_name_number	The H65A mutant diverges significantly from the wild type in the position of the residues Glu32 and Tyr39 in the FOC.	RESULTS
+113	116	FOC	site	The H65A mutant diverges significantly from the wild type in the position of the residues Glu32 and Tyr39 in the FOC.	RESULTS
+0	3	E32	residue_name_number	E32 appears in either the original orientation as the wild type and coordinates Ca2+ in this position, or it is flipped by 180° at the Cβ, moving away from the coordinated calcium ion in the FOC.	RESULTS
+54	63	wild type	protein_state	E32 appears in either the original orientation as the wild type and coordinates Ca2+ in this position, or it is flipped by 180° at the Cβ, moving away from the coordinated calcium ion in the FOC.	RESULTS
+68	79	coordinates	bond_interaction	E32 appears in either the original orientation as the wild type and coordinates Ca2+ in this position, or it is flipped by 180° at the Cβ, moving away from the coordinated calcium ion in the FOC.	RESULTS
+80	84	Ca2+	chemical	E32 appears in either the original orientation as the wild type and coordinates Ca2+ in this position, or it is flipped by 180° at the Cβ, moving away from the coordinated calcium ion in the FOC.	RESULTS
+160	171	coordinated	bond_interaction	E32 appears in either the original orientation as the wild type and coordinates Ca2+ in this position, or it is flipped by 180° at the Cβ, moving away from the coordinated calcium ion in the FOC.	RESULTS
+172	179	calcium	chemical	E32 appears in either the original orientation as the wild type and coordinates Ca2+ in this position, or it is flipped by 180° at the Cβ, moving away from the coordinated calcium ion in the FOC.	RESULTS
+191	194	FOC	site	E32 appears in either the original orientation as the wild type and coordinates Ca2+ in this position, or it is flipped by 180° at the Cβ, moving away from the coordinated calcium ion in the FOC.	RESULTS
+0	5	Tyr39	residue_name_number	Tyr39 moves closer to Ca2+ compared to the wild-type and coordinates the calcium ion (Figure 11—figure supplement 3).	RESULTS
+22	26	Ca2+	chemical	Tyr39 moves closer to Ca2+ compared to the wild-type and coordinates the calcium ion (Figure 11—figure supplement 3).	RESULTS
+43	52	wild-type	protein_state	Tyr39 moves closer to Ca2+ compared to the wild-type and coordinates the calcium ion (Figure 11—figure supplement 3).	RESULTS
+57	68	coordinates	bond_interaction	Tyr39 moves closer to Ca2+ compared to the wild-type and coordinates the calcium ion (Figure 11—figure supplement 3).	RESULTS
+73	80	calcium	chemical	Tyr39 moves closer to Ca2+ compared to the wild-type and coordinates the calcium ion (Figure 11—figure supplement 3).	RESULTS
+9	16	calcium	chemical	A single calcium ion is present in the entry site of this mutant; however, Glu31 of one chain is rotated away from the metal ion and is not involved in coordination.	RESULTS
+39	49	entry site	site	A single calcium ion is present in the entry site of this mutant; however, Glu31 of one chain is rotated away from the metal ion and is not involved in coordination.	RESULTS
+58	64	mutant	protein_state	A single calcium ion is present in the entry site of this mutant; however, Glu31 of one chain is rotated away from the metal ion and is not involved in coordination.	RESULTS
+75	80	Glu31	residue_name_number	A single calcium ion is present in the entry site of this mutant; however, Glu31 of one chain is rotated away from the metal ion and is not involved in coordination.	RESULTS
+152	164	coordination	bond_interaction	A single calcium ion is present in the entry site of this mutant; however, Glu31 of one chain is rotated away from the metal ion and is not involved in coordination.	RESULTS
+70	73	FOC	site	Taken together the results of our data show that these changes to the FOC of EncFtn still permit the formation of the decameric form of the protein.	RESULTS
+77	83	EncFtn	protein	Taken together the results of our data show that these changes to the FOC of EncFtn still permit the formation of the decameric form of the protein.	RESULTS
+118	127	decameric	oligomeric_state	Taken together the results of our data show that these changes to the FOC of EncFtn still permit the formation of the decameric form of the protein.	RESULTS
+30	39	decameric	oligomeric_state	While the proteins all appear decameric in crystals, their solution and gas-phase behavior differs considerably and the mutants no longer show metal-dependent oligomerization.	RESULTS
+43	51	crystals	evidence	While the proteins all appear decameric in crystals, their solution and gas-phase behavior differs considerably and the mutants no longer show metal-dependent oligomerization.	RESULTS
+120	127	mutants	protein_state	While the proteins all appear decameric in crystals, their solution and gas-phase behavior differs considerably and the mutants no longer show metal-dependent oligomerization.	RESULTS
+42	47	metal	chemical	These results highlight the importance of metal coordination in the FOC for the stability and assembly of the EncFtn protein.	RESULTS
+48	60	coordination	bond_interaction	These results highlight the importance of metal coordination in the FOC for the stability and assembly of the EncFtn protein.	RESULTS
+68	71	FOC	site	These results highlight the importance of metal coordination in the FOC for the stability and assembly of the EncFtn protein.	RESULTS
+110	116	EncFtn	protein	These results highlight the importance of metal coordination in the FOC for the stability and assembly of the EncFtn protein.	RESULTS
+0	15	Progress curves	evidence	Progress curves recording ferroxidase activity of EncFtnsH mutants.	FIG
+26	37	ferroxidase	protein_type	Progress curves recording ferroxidase activity of EncFtnsH mutants.	FIG
+50	58	EncFtnsH	protein	Progress curves recording ferroxidase activity of EncFtnsH mutants.	FIG
+59	66	mutants	protein_state	Progress curves recording ferroxidase activity of EncFtnsH mutants.	FIG
+6	15	wild-type	protein_state	20 µM wild-type EncFtnsH, E32A, E62A and H65A mutants were mixed with 20 µM or 100 µM acidic Fe(NH4)2(SO4)2, respectively.	FIG
+16	24	EncFtnsH	protein	20 µM wild-type EncFtnsH, E32A, E62A and H65A mutants were mixed with 20 µM or 100 µM acidic Fe(NH4)2(SO4)2, respectively.	FIG
+26	30	E32A	mutant	20 µM wild-type EncFtnsH, E32A, E62A and H65A mutants were mixed with 20 µM or 100 µM acidic Fe(NH4)2(SO4)2, respectively.	FIG
+32	36	E62A	mutant	20 µM wild-type EncFtnsH, E32A, E62A and H65A mutants were mixed with 20 µM or 100 µM acidic Fe(NH4)2(SO4)2, respectively.	FIG
+41	45	H65A	mutant	20 µM wild-type EncFtnsH, E32A, E62A and H65A mutants were mixed with 20 µM or 100 µM acidic Fe(NH4)2(SO4)2, respectively.	FIG
+46	53	mutants	protein_state	20 µM wild-type EncFtnsH, E32A, E62A and H65A mutants were mixed with 20 µM or 100 µM acidic Fe(NH4)2(SO4)2, respectively.	FIG
+93	107	Fe(NH4)2(SO4)2	chemical	20 µM wild-type EncFtnsH, E32A, E62A and H65A mutants were mixed with 20 µM or 100 µM acidic Fe(NH4)2(SO4)2, respectively.	FIG
+73	77	Fe3+	chemical	Absorbance at 315 nm was recorded for 1800 s at 25°C as an indication of Fe3+ formation.	FIG
+65	69	Fe2+	chemical	Protein free samples (dashed and dotted lines) were measured for Fe2+ background oxidation as controls.	FIG
+9	20	ferroxidase	protein_type	Relative ferroxidase activity of EncFtnsH mutants.	FIG
+33	41	EncFtnsH	protein	Relative ferroxidase activity of EncFtnsH mutants.	FIG
+42	49	mutants	protein_state	Relative ferroxidase activity of EncFtnsH mutants.	FIG
+0	8	EncFtnsH	protein	EncFtnsH, and the mutant forms E32A, E62A and H65A, each at 20 µM, were mixed with 100 µM acidic Fe(NH4)2(SO4)2.	FIG
+18	24	mutant	protein_state	EncFtnsH, and the mutant forms E32A, E62A and H65A, each at 20 µM, were mixed with 100 µM acidic Fe(NH4)2(SO4)2.	FIG
+31	35	E32A	mutant	EncFtnsH, and the mutant forms E32A, E62A and H65A, each at 20 µM, were mixed with 100 µM acidic Fe(NH4)2(SO4)2.	FIG
+37	41	E62A	mutant	EncFtnsH, and the mutant forms E32A, E62A and H65A, each at 20 µM, were mixed with 100 µM acidic Fe(NH4)2(SO4)2.	FIG
+46	50	H65A	mutant	EncFtnsH, and the mutant forms E32A, E62A and H65A, each at 20 µM, were mixed with 100 µM acidic Fe(NH4)2(SO4)2.	FIG
+97	111	Fe(NH4)2(SO4)2	chemical	EncFtnsH, and the mutant forms E32A, E62A and H65A, each at 20 µM, were mixed with 100 µM acidic Fe(NH4)2(SO4)2.	FIG
+0	11	Ferroxidase	protein_type	Ferroxidase activity of the mutant forms is determined by measuring the absorbance at 315 nm for 1800 s at 25 °C as an indication of Fe3+ formation.	FIG
+28	34	mutant	protein_state	Ferroxidase activity of the mutant forms is determined by measuring the absorbance at 315 nm for 1800 s at 25 °C as an indication of Fe3+ formation.	FIG
+58	92	measuring the absorbance at 315 nm	experimental_method	Ferroxidase activity of the mutant forms is determined by measuring the absorbance at 315 nm for 1800 s at 25 °C as an indication of Fe3+ formation.	FIG
+133	137	Fe3+	chemical	Ferroxidase activity of the mutant forms is determined by measuring the absorbance at 315 nm for 1800 s at 25 °C as an indication of Fe3+ formation.	FIG
+13	24	ferroxidase	protein_type	The relative ferroxidase activity of mutants is plotted as a proportion of the activity of the wild-type protein using the endpoint measurement of A315.	FIG
+37	44	mutants	protein_state	The relative ferroxidase activity of mutants is plotted as a proportion of the activity of the wild-type protein using the endpoint measurement of A315.	FIG
+95	104	wild-type	protein_state	The relative ferroxidase activity of mutants is plotted as a proportion of the activity of the wild-type protein using the endpoint measurement of A315.	FIG
+132	151	measurement of A315	experimental_method	The relative ferroxidase activity of mutants is plotted as a proportion of the activity of the wild-type protein using the endpoint measurement of A315.	FIG
+4	7	FOC	site	The FOC mutants showed reduced ferroxidase activity to varied extents, among which E62A significantly abrogated the ferroxidase activity.	FIG
+8	15	mutants	protein_state	The FOC mutants showed reduced ferroxidase activity to varied extents, among which E62A significantly abrogated the ferroxidase activity.	FIG
+31	42	ferroxidase	protein_type	The FOC mutants showed reduced ferroxidase activity to varied extents, among which E62A significantly abrogated the ferroxidase activity.	FIG
+83	87	E62A	mutant	The FOC mutants showed reduced ferroxidase activity to varied extents, among which E62A significantly abrogated the ferroxidase activity.	FIG
+116	127	ferroxidase	protein_type	The FOC mutants showed reduced ferroxidase activity to varied extents, among which E62A significantly abrogated the ferroxidase activity.	FIG
+31	42	mutagenesis	experimental_method	To address the question of how mutagenesis of the iron coordinating residues affects the enzymatic activity of the EncFtnsH protein we recorded progress curves for the oxidation of Fe2+ to Fe3+ by the different mutants as before.	RESULTS
+50	76	iron coordinating residues	site	To address the question of how mutagenesis of the iron coordinating residues affects the enzymatic activity of the EncFtnsH protein we recorded progress curves for the oxidation of Fe2+ to Fe3+ by the different mutants as before.	RESULTS
+115	123	EncFtnsH	protein	To address the question of how mutagenesis of the iron coordinating residues affects the enzymatic activity of the EncFtnsH protein we recorded progress curves for the oxidation of Fe2+ to Fe3+ by the different mutants as before.	RESULTS
+144	159	progress curves	evidence	To address the question of how mutagenesis of the iron coordinating residues affects the enzymatic activity of the EncFtnsH protein we recorded progress curves for the oxidation of Fe2+ to Fe3+ by the different mutants as before.	RESULTS
+181	185	Fe2+	chemical	To address the question of how mutagenesis of the iron coordinating residues affects the enzymatic activity of the EncFtnsH protein we recorded progress curves for the oxidation of Fe2+ to Fe3+ by the different mutants as before.	RESULTS
+189	193	Fe3+	chemical	To address the question of how mutagenesis of the iron coordinating residues affects the enzymatic activity of the EncFtnsH protein we recorded progress curves for the oxidation of Fe2+ to Fe3+ by the different mutants as before.	RESULTS
+211	218	mutants	protein_state	To address the question of how mutagenesis of the iron coordinating residues affects the enzymatic activity of the EncFtnsH protein we recorded progress curves for the oxidation of Fe2+ to Fe3+ by the different mutants as before.	RESULTS
+0	11	Mutagenesis	experimental_method	Mutagenesis of E32A and H65A reduces the activity of EncFtnsH by about 40%-55%; the E62A mutant completely abrogates activity, presumably through the loss of the bridging coordination for the formation of the di-nuclear iron center of the FOC (Figure 12).	RESULTS
+15	19	E32A	mutant	Mutagenesis of E32A and H65A reduces the activity of EncFtnsH by about 40%-55%; the E62A mutant completely abrogates activity, presumably through the loss of the bridging coordination for the formation of the di-nuclear iron center of the FOC (Figure 12).	RESULTS
+24	28	H65A	mutant	Mutagenesis of E32A and H65A reduces the activity of EncFtnsH by about 40%-55%; the E62A mutant completely abrogates activity, presumably through the loss of the bridging coordination for the formation of the di-nuclear iron center of the FOC (Figure 12).	RESULTS
+53	61	EncFtnsH	protein	Mutagenesis of E32A and H65A reduces the activity of EncFtnsH by about 40%-55%; the E62A mutant completely abrogates activity, presumably through the loss of the bridging coordination for the formation of the di-nuclear iron center of the FOC (Figure 12).	RESULTS
+84	88	E62A	mutant	Mutagenesis of E32A and H65A reduces the activity of EncFtnsH by about 40%-55%; the E62A mutant completely abrogates activity, presumably through the loss of the bridging coordination for the formation of the di-nuclear iron center of the FOC (Figure 12).	RESULTS
+89	95	mutant	protein_state	Mutagenesis of E32A and H65A reduces the activity of EncFtnsH by about 40%-55%; the E62A mutant completely abrogates activity, presumably through the loss of the bridging coordination for the formation of the di-nuclear iron center of the FOC (Figure 12).	RESULTS
+150	157	loss of	protein_state	Mutagenesis of E32A and H65A reduces the activity of EncFtnsH by about 40%-55%; the E62A mutant completely abrogates activity, presumably through the loss of the bridging coordination for the formation of the di-nuclear iron center of the FOC (Figure 12).	RESULTS
+171	183	coordination	bond_interaction	Mutagenesis of E32A and H65A reduces the activity of EncFtnsH by about 40%-55%; the E62A mutant completely abrogates activity, presumably through the loss of the bridging coordination for the formation of the di-nuclear iron center of the FOC (Figure 12).	RESULTS
+209	231	di-nuclear iron center	site	Mutagenesis of E32A and H65A reduces the activity of EncFtnsH by about 40%-55%; the E62A mutant completely abrogates activity, presumably through the loss of the bridging coordination for the formation of the di-nuclear iron center of the FOC (Figure 12).	RESULTS
+239	242	FOC	site	Mutagenesis of E32A and H65A reduces the activity of EncFtnsH by about 40%-55%; the E62A mutant completely abrogates activity, presumably through the loss of the bridging coordination for the formation of the di-nuclear iron center of the FOC (Figure 12).	RESULTS
+28	36	mutating	experimental_method	Collectively, the effect of mutating these residues in the FOC confirms the importance of the iron coordinating residues for the ferroxidase activity of the EncFtnsH protein.	RESULTS
+59	62	FOC	site	Collectively, the effect of mutating these residues in the FOC confirms the importance of the iron coordinating residues for the ferroxidase activity of the EncFtnsH protein.	RESULTS
+94	120	iron coordinating residues	site	Collectively, the effect of mutating these residues in the FOC confirms the importance of the iron coordinating residues for the ferroxidase activity of the EncFtnsH protein.	RESULTS
+129	140	ferroxidase	protein_type	Collectively, the effect of mutating these residues in the FOC confirms the importance of the iron coordinating residues for the ferroxidase activity of the EncFtnsH protein.	RESULTS
+157	165	EncFtnsH	protein	Collectively, the effect of mutating these residues in the FOC confirms the importance of the iron coordinating residues for the ferroxidase activity of the EncFtnsH protein.	RESULTS
+0	17	Phylogenetic tree	evidence	Phylogenetic tree of ferritin family proteins.	FIG
+21	29	ferritin	protein_type	Phylogenetic tree of ferritin family proteins.	FIG
+29	52	Neighbor-Joining method	experimental_method	The tree was built using the Neighbor-Joining method based on step-wise amino acid sequence alignment of the four-helical bundle portions of ferritin family proteins (Supplementary file 1).	FIG
+62	101	step-wise amino acid sequence alignment	experimental_method	The tree was built using the Neighbor-Joining method based on step-wise amino acid sequence alignment of the four-helical bundle portions of ferritin family proteins (Supplementary file 1).	FIG
+109	128	four-helical bundle	structure_element	The tree was built using the Neighbor-Joining method based on step-wise amino acid sequence alignment of the four-helical bundle portions of ferritin family proteins (Supplementary file 1).	FIG
+141	149	ferritin	protein_type	The tree was built using the Neighbor-Joining method based on step-wise amino acid sequence alignment of the four-helical bundle portions of ferritin family proteins (Supplementary file 1).	FIG
+4	26	evolutionary distances	evidence	The evolutionary distances were computed using the p-distance method and are in the units of the number of amino acid differences per site.	FIG
+51	68	p-distance method	experimental_method	The evolutionary distances were computed using the p-distance method and are in the units of the number of amino acid differences per site.	FIG
+36	44	ferritin	protein_type	Our study reports on a new class of ferritin-like proteins (EncFtn), which are associated with bacterial encapsulin nanocompartments (Enc).	DISCUSS
+60	66	EncFtn	protein	Our study reports on a new class of ferritin-like proteins (EncFtn), which are associated with bacterial encapsulin nanocompartments (Enc).	DISCUSS
+95	104	bacterial	taxonomy_domain	Our study reports on a new class of ferritin-like proteins (EncFtn), which are associated with bacterial encapsulin nanocompartments (Enc).	DISCUSS
+105	115	encapsulin	protein	Our study reports on a new class of ferritin-like proteins (EncFtn), which are associated with bacterial encapsulin nanocompartments (Enc).	DISCUSS
+116	132	nanocompartments	complex_assembly	Our study reports on a new class of ferritin-like proteins (EncFtn), which are associated with bacterial encapsulin nanocompartments (Enc).	DISCUSS
+134	137	Enc	protein	Our study reports on a new class of ferritin-like proteins (EncFtn), which are associated with bacterial encapsulin nanocompartments (Enc).	DISCUSS
+16	22	EncFtn	protein	By studying the EncFtn from R. rubrum we demonstrate that iron binding results in assembly of EncFtn decamers, which display a unique annular architecture.	DISCUSS
+28	37	R. rubrum	species	By studying the EncFtn from R. rubrum we demonstrate that iron binding results in assembly of EncFtn decamers, which display a unique annular architecture.	DISCUSS
+58	62	iron	chemical	By studying the EncFtn from R. rubrum we demonstrate that iron binding results in assembly of EncFtn decamers, which display a unique annular architecture.	DISCUSS
+94	100	EncFtn	protein	By studying the EncFtn from R. rubrum we demonstrate that iron binding results in assembly of EncFtn decamers, which display a unique annular architecture.	DISCUSS
+101	109	decamers	oligomeric_state	By studying the EncFtn from R. rubrum we demonstrate that iron binding results in assembly of EncFtn decamers, which display a unique annular architecture.	DISCUSS
+58	67	classical	protein_state	Despite a radically different quaternary structure to the classical ferritins, the four-helical bundle scaffold and FOC of EncFtnsH are strikingly similar to ferritin (Figure 6A).	DISCUSS
+68	77	ferritins	protein_type	Despite a radically different quaternary structure to the classical ferritins, the four-helical bundle scaffold and FOC of EncFtnsH are strikingly similar to ferritin (Figure 6A).	DISCUSS
+83	111	four-helical bundle scaffold	structure_element	Despite a radically different quaternary structure to the classical ferritins, the four-helical bundle scaffold and FOC of EncFtnsH are strikingly similar to ferritin (Figure 6A).	DISCUSS
+116	119	FOC	site	Despite a radically different quaternary structure to the classical ferritins, the four-helical bundle scaffold and FOC of EncFtnsH are strikingly similar to ferritin (Figure 6A).	DISCUSS
+123	131	EncFtnsH	protein	Despite a radically different quaternary structure to the classical ferritins, the four-helical bundle scaffold and FOC of EncFtnsH are strikingly similar to ferritin (Figure 6A).	DISCUSS
+158	166	ferritin	protein_type	Despite a radically different quaternary structure to the classical ferritins, the four-helical bundle scaffold and FOC of EncFtnsH are strikingly similar to ferritin (Figure 6A).	DISCUSS
+2	34	sequence-based phylogenetic tree	experimental_method	A sequence-based phylogenetic tree for proteins in the ferritin family was constructed; in addition to the classical ferritins, bacterioferritins and Dps proteins, our analysis included the encapsulin-associated ferritin-like proteins (EncFtns) and a group related to these, but lacking the encapsulin sequence (Non-EncFtn).	DISCUSS
+55	63	ferritin	protein_type	A sequence-based phylogenetic tree for proteins in the ferritin family was constructed; in addition to the classical ferritins, bacterioferritins and Dps proteins, our analysis included the encapsulin-associated ferritin-like proteins (EncFtns) and a group related to these, but lacking the encapsulin sequence (Non-EncFtn).	DISCUSS
+107	116	classical	protein_state	A sequence-based phylogenetic tree for proteins in the ferritin family was constructed; in addition to the classical ferritins, bacterioferritins and Dps proteins, our analysis included the encapsulin-associated ferritin-like proteins (EncFtns) and a group related to these, but lacking the encapsulin sequence (Non-EncFtn).	DISCUSS
+117	126	ferritins	protein_type	A sequence-based phylogenetic tree for proteins in the ferritin family was constructed; in addition to the classical ferritins, bacterioferritins and Dps proteins, our analysis included the encapsulin-associated ferritin-like proteins (EncFtns) and a group related to these, but lacking the encapsulin sequence (Non-EncFtn).	DISCUSS
+128	145	bacterioferritins	protein_type	A sequence-based phylogenetic tree for proteins in the ferritin family was constructed; in addition to the classical ferritins, bacterioferritins and Dps proteins, our analysis included the encapsulin-associated ferritin-like proteins (EncFtns) and a group related to these, but lacking the encapsulin sequence (Non-EncFtn).	DISCUSS
+150	153	Dps	protein_type	A sequence-based phylogenetic tree for proteins in the ferritin family was constructed; in addition to the classical ferritins, bacterioferritins and Dps proteins, our analysis included the encapsulin-associated ferritin-like proteins (EncFtns) and a group related to these, but lacking the encapsulin sequence (Non-EncFtn).	DISCUSS
+190	234	encapsulin-associated ferritin-like proteins	protein_type	A sequence-based phylogenetic tree for proteins in the ferritin family was constructed; in addition to the classical ferritins, bacterioferritins and Dps proteins, our analysis included the encapsulin-associated ferritin-like proteins (EncFtns) and a group related to these, but lacking the encapsulin sequence (Non-EncFtn).	DISCUSS
+236	243	EncFtns	protein_type	A sequence-based phylogenetic tree for proteins in the ferritin family was constructed; in addition to the classical ferritins, bacterioferritins and Dps proteins, our analysis included the encapsulin-associated ferritin-like proteins (EncFtns) and a group related to these, but lacking the encapsulin sequence (Non-EncFtn).	DISCUSS
+291	301	encapsulin	protein	A sequence-based phylogenetic tree for proteins in the ferritin family was constructed; in addition to the classical ferritins, bacterioferritins and Dps proteins, our analysis included the encapsulin-associated ferritin-like proteins (EncFtns) and a group related to these, but lacking the encapsulin sequence (Non-EncFtn).	DISCUSS
+312	322	Non-EncFtn	protein_type	A sequence-based phylogenetic tree for proteins in the ferritin family was constructed; in addition to the classical ferritins, bacterioferritins and Dps proteins, our analysis included the encapsulin-associated ferritin-like proteins (EncFtns) and a group related to these, but lacking the encapsulin sequence (Non-EncFtn).	DISCUSS
+31	37	EncFtn	protein	The analysis revealed that the EncFtn and Non-EncFtn proteins form groups distinct from the other clearly delineated groups of ferritins, and represent outliers in the tree (Figure 13).	DISCUSS
+42	52	Non-EncFtn	protein_type	The analysis revealed that the EncFtn and Non-EncFtn proteins form groups distinct from the other clearly delineated groups of ferritins, and represent outliers in the tree (Figure 13).	DISCUSS
+127	136	ferritins	protein_type	The analysis revealed that the EncFtn and Non-EncFtn proteins form groups distinct from the other clearly delineated groups of ferritins, and represent outliers in the tree (Figure 13).	DISCUSS
+98	118	active site scaffold	site	While it is difficult to infer ancestral lineages in protein families, the similarity seen in the active site scaffold of these proteins highlights a shared evolutionary relationship between EncFtn proteins and other members of the ferritin superfamily that has been noted in previous studies (; ).	DISCUSS
+191	197	EncFtn	protein_type	While it is difficult to infer ancestral lineages in protein families, the similarity seen in the active site scaffold of these proteins highlights a shared evolutionary relationship between EncFtn proteins and other members of the ferritin superfamily that has been noted in previous studies (; ).	DISCUSS
+232	240	ferritin	protein_type	While it is difficult to infer ancestral lineages in protein families, the similarity seen in the active site scaffold of these proteins highlights a shared evolutionary relationship between EncFtn proteins and other members of the ferritin superfamily that has been noted in previous studies (; ).	DISCUSS
+40	57	four-helical fold	structure_element	From this analysis, we propose that the four-helical fold of the classical ferritins may have arisen through gene duplication of an ancestor of EncFtn.	DISCUSS
+65	74	classical	protein_state	From this analysis, we propose that the four-helical fold of the classical ferritins may have arisen through gene duplication of an ancestor of EncFtn.	DISCUSS
+75	84	ferritins	protein_type	From this analysis, we propose that the four-helical fold of the classical ferritins may have arisen through gene duplication of an ancestor of EncFtn.	DISCUSS
+144	150	EncFtn	protein	From this analysis, we propose that the four-helical fold of the classical ferritins may have arisen through gene duplication of an ancestor of EncFtn.	DISCUSS
+42	59	C-terminal region	structure_element	This gene duplication would result in the C-terminal region of one EncFtn monomer being linked to the N-terminus of another and thus stabilizing the four-helix bundle fold within a single polypeptide chain (Figure 6B).	DISCUSS
+67	73	EncFtn	protein	This gene duplication would result in the C-terminal region of one EncFtn monomer being linked to the N-terminus of another and thus stabilizing the four-helix bundle fold within a single polypeptide chain (Figure 6B).	DISCUSS
+74	81	monomer	oligomeric_state	This gene duplication would result in the C-terminal region of one EncFtn monomer being linked to the N-terminus of another and thus stabilizing the four-helix bundle fold within a single polypeptide chain (Figure 6B).	DISCUSS
+149	171	four-helix bundle fold	structure_element	This gene duplication would result in the C-terminal region of one EncFtn monomer being linked to the N-terminus of another and thus stabilizing the four-helix bundle fold within a single polypeptide chain (Figure 6B).	DISCUSS
+102	105	FOC	site	Linking the protein together in this way relaxes the requirement for the maintenance of a symmetrical FOC and thus provides a path to the diversity in active-site residues seen across the ferritin family (Figure 6A, residues Glu95, Gln128 and Glu131 in PmFtn, Supplementary file 1).	DISCUSS
+151	171	active-site residues	site	Linking the protein together in this way relaxes the requirement for the maintenance of a symmetrical FOC and thus provides a path to the diversity in active-site residues seen across the ferritin family (Figure 6A, residues Glu95, Gln128 and Glu131 in PmFtn, Supplementary file 1).	DISCUSS
+188	196	ferritin	protein_type	Linking the protein together in this way relaxes the requirement for the maintenance of a symmetrical FOC and thus provides a path to the diversity in active-site residues seen across the ferritin family (Figure 6A, residues Glu95, Gln128 and Glu131 in PmFtn, Supplementary file 1).	DISCUSS
+225	230	Glu95	residue_name_number	Linking the protein together in this way relaxes the requirement for the maintenance of a symmetrical FOC and thus provides a path to the diversity in active-site residues seen across the ferritin family (Figure 6A, residues Glu95, Gln128 and Glu131 in PmFtn, Supplementary file 1).	DISCUSS
+232	238	Gln128	residue_name_number	Linking the protein together in this way relaxes the requirement for the maintenance of a symmetrical FOC and thus provides a path to the diversity in active-site residues seen across the ferritin family (Figure 6A, residues Glu95, Gln128 and Glu131 in PmFtn, Supplementary file 1).	DISCUSS
+243	249	Glu131	residue_name_number	Linking the protein together in this way relaxes the requirement for the maintenance of a symmetrical FOC and thus provides a path to the diversity in active-site residues seen across the ferritin family (Figure 6A, residues Glu95, Gln128 and Glu131 in PmFtn, Supplementary file 1).	DISCUSS
+253	258	PmFtn	protein	Linking the protein together in this way relaxes the requirement for the maintenance of a symmetrical FOC and thus provides a path to the diversity in active-site residues seen across the ferritin family (Figure 6A, residues Glu95, Gln128 and Glu131 in PmFtn, Supplementary file 1).	DISCUSS
+21	29	ferritin	protein_type	Relationship between ferritin structure and activity	DISCUSS
+30	39	structure	evidence	Relationship between ferritin structure and activity	DISCUSS
+30	39	classical	protein_state	The quaternary arrangement of classical ferritins into an octahedral nanocage and Dps into a dodecamer is absolutely required for their function as iron storage compartments.	DISCUSS
+40	49	ferritins	protein_type	The quaternary arrangement of classical ferritins into an octahedral nanocage and Dps into a dodecamer is absolutely required for their function as iron storage compartments.	DISCUSS
+58	68	octahedral	protein_state	The quaternary arrangement of classical ferritins into an octahedral nanocage and Dps into a dodecamer is absolutely required for their function as iron storage compartments.	DISCUSS
+69	77	nanocage	complex_assembly	The quaternary arrangement of classical ferritins into an octahedral nanocage and Dps into a dodecamer is absolutely required for their function as iron storage compartments.	DISCUSS
+82	85	Dps	protein	The quaternary arrangement of classical ferritins into an octahedral nanocage and Dps into a dodecamer is absolutely required for their function as iron storage compartments.	DISCUSS
+93	102	dodecamer	oligomeric_state	The quaternary arrangement of classical ferritins into an octahedral nanocage and Dps into a dodecamer is absolutely required for their function as iron storage compartments.	DISCUSS
+148	152	iron	chemical	The quaternary arrangement of classical ferritins into an octahedral nanocage and Dps into a dodecamer is absolutely required for their function as iron storage compartments.	DISCUSS
+36	40	iron	chemical	The oxidation and mineralization of iron must be spatially separated from the host cytosol to prevent the formation of damaging hydroxyl radicals in the Fenton and Haber-Weiss reactions.	DISCUSS
+25	34	ferritins	protein_type	 This is achieved in all ferritins by confining the oxidation of iron to the interior of the protein complex, thus achieving sequestration of the Fe3+ mineralization product.	DISCUSS
+65	69	iron	chemical	 This is achieved in all ferritins by confining the oxidation of iron to the interior of the protein complex, thus achieving sequestration of the Fe3+ mineralization product.	DISCUSS
+146	150	Fe3+	chemical	 This is achieved in all ferritins by confining the oxidation of iron to the interior of the protein complex, thus achieving sequestration of the Fe3+ mineralization product.	DISCUSS
+2	22	structural alignment	experimental_method	A structural alignment of the FOC of EncFtn with the classical ferritin PmFtn shows that the central ring of EncFtn corresponds to the external surface of ferritin, while the outer circumference of EncFtn is congruent with the inner mineralization surface of ferritin (Figure 6—figure supplement 1A).	DISCUSS
+30	33	FOC	site	A structural alignment of the FOC of EncFtn with the classical ferritin PmFtn shows that the central ring of EncFtn corresponds to the external surface of ferritin, while the outer circumference of EncFtn is congruent with the inner mineralization surface of ferritin (Figure 6—figure supplement 1A).	DISCUSS
+37	43	EncFtn	protein	A structural alignment of the FOC of EncFtn with the classical ferritin PmFtn shows that the central ring of EncFtn corresponds to the external surface of ferritin, while the outer circumference of EncFtn is congruent with the inner mineralization surface of ferritin (Figure 6—figure supplement 1A).	DISCUSS
+53	62	classical	protein_state	A structural alignment of the FOC of EncFtn with the classical ferritin PmFtn shows that the central ring of EncFtn corresponds to the external surface of ferritin, while the outer circumference of EncFtn is congruent with the inner mineralization surface of ferritin (Figure 6—figure supplement 1A).	DISCUSS
+63	71	ferritin	protein_type	A structural alignment of the FOC of EncFtn with the classical ferritin PmFtn shows that the central ring of EncFtn corresponds to the external surface of ferritin, while the outer circumference of EncFtn is congruent with the inner mineralization surface of ferritin (Figure 6—figure supplement 1A).	DISCUSS
+72	77	PmFtn	protein	A structural alignment of the FOC of EncFtn with the classical ferritin PmFtn shows that the central ring of EncFtn corresponds to the external surface of ferritin, while the outer circumference of EncFtn is congruent with the inner mineralization surface of ferritin (Figure 6—figure supplement 1A).	DISCUSS
+93	105	central ring	structure_element	A structural alignment of the FOC of EncFtn with the classical ferritin PmFtn shows that the central ring of EncFtn corresponds to the external surface of ferritin, while the outer circumference of EncFtn is congruent with the inner mineralization surface of ferritin (Figure 6—figure supplement 1A).	DISCUSS
+109	115	EncFtn	protein	A structural alignment of the FOC of EncFtn with the classical ferritin PmFtn shows that the central ring of EncFtn corresponds to the external surface of ferritin, while the outer circumference of EncFtn is congruent with the inner mineralization surface of ferritin (Figure 6—figure supplement 1A).	DISCUSS
+155	163	ferritin	protein_type	A structural alignment of the FOC of EncFtn with the classical ferritin PmFtn shows that the central ring of EncFtn corresponds to the external surface of ferritin, while the outer circumference of EncFtn is congruent with the inner mineralization surface of ferritin (Figure 6—figure supplement 1A).	DISCUSS
+198	204	EncFtn	protein	A structural alignment of the FOC of EncFtn with the classical ferritin PmFtn shows that the central ring of EncFtn corresponds to the external surface of ferritin, while the outer circumference of EncFtn is congruent with the inner mineralization surface of ferritin (Figure 6—figure supplement 1A).	DISCUSS
+233	255	mineralization surface	site	A structural alignment of the FOC of EncFtn with the classical ferritin PmFtn shows that the central ring of EncFtn corresponds to the external surface of ferritin, while the outer circumference of EncFtn is congruent with the inner mineralization surface of ferritin (Figure 6—figure supplement 1A).	DISCUSS
+259	267	ferritin	protein_type	A structural alignment of the FOC of EncFtn with the classical ferritin PmFtn shows that the central ring of EncFtn corresponds to the external surface of ferritin, while the outer circumference of EncFtn is congruent with the inner mineralization surface of ferritin (Figure 6—figure supplement 1A).	DISCUSS
+5	12	overlay	experimental_method	This overlay highlights the fact that the ferroxidase center of EncFtn faces in the opposite direction relative to the classical ferritins and is essentially inside out regarding iron storage space (Figure 6—figure supplement 1B, boxed region).	DISCUSS
+42	60	ferroxidase center	site	This overlay highlights the fact that the ferroxidase center of EncFtn faces in the opposite direction relative to the classical ferritins and is essentially inside out regarding iron storage space (Figure 6—figure supplement 1B, boxed region).	DISCUSS
+64	70	EncFtn	protein	This overlay highlights the fact that the ferroxidase center of EncFtn faces in the opposite direction relative to the classical ferritins and is essentially inside out regarding iron storage space (Figure 6—figure supplement 1B, boxed region).	DISCUSS
+119	128	classical	protein_state	This overlay highlights the fact that the ferroxidase center of EncFtn faces in the opposite direction relative to the classical ferritins and is essentially inside out regarding iron storage space (Figure 6—figure supplement 1B, boxed region).	DISCUSS
+129	138	ferritins	protein_type	This overlay highlights the fact that the ferroxidase center of EncFtn faces in the opposite direction relative to the classical ferritins and is essentially inside out regarding iron storage space (Figure 6—figure supplement 1B, boxed region).	DISCUSS
+179	183	iron	chemical	This overlay highlights the fact that the ferroxidase center of EncFtn faces in the opposite direction relative to the classical ferritins and is essentially inside out regarding iron storage space (Figure 6—figure supplement 1B, boxed region).	DISCUSS
+31	40	mutations	experimental_method	Analysis of each of the single mutations (E32A, E62A and H65A) made in the FOC highlights the importance of the iron-coordinating residues in the catalytic activity of EncFtn.	DISCUSS
+42	46	E32A	mutant	Analysis of each of the single mutations (E32A, E62A and H65A) made in the FOC highlights the importance of the iron-coordinating residues in the catalytic activity of EncFtn.	DISCUSS
+48	52	E62A	mutant	Analysis of each of the single mutations (E32A, E62A and H65A) made in the FOC highlights the importance of the iron-coordinating residues in the catalytic activity of EncFtn.	DISCUSS
+57	61	H65A	mutant	Analysis of each of the single mutations (E32A, E62A and H65A) made in the FOC highlights the importance of the iron-coordinating residues in the catalytic activity of EncFtn.	DISCUSS
+75	78	FOC	site	Analysis of each of the single mutations (E32A, E62A and H65A) made in the FOC highlights the importance of the iron-coordinating residues in the catalytic activity of EncFtn.	DISCUSS
+112	138	iron-coordinating residues	site	Analysis of each of the single mutations (E32A, E62A and H65A) made in the FOC highlights the importance of the iron-coordinating residues in the catalytic activity of EncFtn.	DISCUSS
+168	174	EncFtn	protein	Analysis of each of the single mutations (E32A, E62A and H65A) made in the FOC highlights the importance of the iron-coordinating residues in the catalytic activity of EncFtn.	DISCUSS
+33	40	calcium	chemical	Furthermore, the position of the calcium ion coordinated by Glu31 and Glu34 seen in the EncFtnsH structure suggests an entry site to channel metal ions into the FOC; we propose that this site binds hydrated iron ions in vivo and acts as a selectivity filter and gate for the FOC.	DISCUSS
+45	59	coordinated by	bond_interaction	Furthermore, the position of the calcium ion coordinated by Glu31 and Glu34 seen in the EncFtnsH structure suggests an entry site to channel metal ions into the FOC; we propose that this site binds hydrated iron ions in vivo and acts as a selectivity filter and gate for the FOC.	DISCUSS
+60	65	Glu31	residue_name_number	Furthermore, the position of the calcium ion coordinated by Glu31 and Glu34 seen in the EncFtnsH structure suggests an entry site to channel metal ions into the FOC; we propose that this site binds hydrated iron ions in vivo and acts as a selectivity filter and gate for the FOC.	DISCUSS
+70	75	Glu34	residue_name_number	Furthermore, the position of the calcium ion coordinated by Glu31 and Glu34 seen in the EncFtnsH structure suggests an entry site to channel metal ions into the FOC; we propose that this site binds hydrated iron ions in vivo and acts as a selectivity filter and gate for the FOC.	DISCUSS
+88	96	EncFtnsH	protein	Furthermore, the position of the calcium ion coordinated by Glu31 and Glu34 seen in the EncFtnsH structure suggests an entry site to channel metal ions into the FOC; we propose that this site binds hydrated iron ions in vivo and acts as a selectivity filter and gate for the FOC.	DISCUSS
+97	106	structure	evidence	Furthermore, the position of the calcium ion coordinated by Glu31 and Glu34 seen in the EncFtnsH structure suggests an entry site to channel metal ions into the FOC; we propose that this site binds hydrated iron ions in vivo and acts as a selectivity filter and gate for the FOC.	DISCUSS
+119	129	entry site	site	Furthermore, the position of the calcium ion coordinated by Glu31 and Glu34 seen in the EncFtnsH structure suggests an entry site to channel metal ions into the FOC; we propose that this site binds hydrated iron ions in vivo and acts as a selectivity filter and gate for the FOC.	DISCUSS
+161	164	FOC	site	Furthermore, the position of the calcium ion coordinated by Glu31 and Glu34 seen in the EncFtnsH structure suggests an entry site to channel metal ions into the FOC; we propose that this site binds hydrated iron ions in vivo and acts as a selectivity filter and gate for the FOC.	DISCUSS
+207	211	iron	chemical	Furthermore, the position of the calcium ion coordinated by Glu31 and Glu34 seen in the EncFtnsH structure suggests an entry site to channel metal ions into the FOC; we propose that this site binds hydrated iron ions in vivo and acts as a selectivity filter and gate for the FOC.	DISCUSS
+275	278	FOC	site	Furthermore, the position of the calcium ion coordinated by Glu31 and Glu34 seen in the EncFtnsH structure suggests an entry site to channel metal ions into the FOC; we propose that this site binds hydrated iron ions in vivo and acts as a selectivity filter and gate for the FOC.	DISCUSS
+68	74	EncFtn	protein	The constellation of charged residues on the outer circumference of EncFtn (His57, Glu61 and Glu64) could function in the same way as the residues lining the mineralization surface within the classical ferritin nanocage, and given their proximity to the FOC these sites may be the exit portal and mineralization site.	DISCUSS
+76	81	His57	residue_name_number	The constellation of charged residues on the outer circumference of EncFtn (His57, Glu61 and Glu64) could function in the same way as the residues lining the mineralization surface within the classical ferritin nanocage, and given their proximity to the FOC these sites may be the exit portal and mineralization site.	DISCUSS
+83	88	Glu61	residue_name_number	The constellation of charged residues on the outer circumference of EncFtn (His57, Glu61 and Glu64) could function in the same way as the residues lining the mineralization surface within the classical ferritin nanocage, and given their proximity to the FOC these sites may be the exit portal and mineralization site.	DISCUSS
+93	98	Glu64	residue_name_number	The constellation of charged residues on the outer circumference of EncFtn (His57, Glu61 and Glu64) could function in the same way as the residues lining the mineralization surface within the classical ferritin nanocage, and given their proximity to the FOC these sites may be the exit portal and mineralization site.	DISCUSS
+158	180	mineralization surface	site	The constellation of charged residues on the outer circumference of EncFtn (His57, Glu61 and Glu64) could function in the same way as the residues lining the mineralization surface within the classical ferritin nanocage, and given their proximity to the FOC these sites may be the exit portal and mineralization site.	DISCUSS
+192	201	classical	protein_state	The constellation of charged residues on the outer circumference of EncFtn (His57, Glu61 and Glu64) could function in the same way as the residues lining the mineralization surface within the classical ferritin nanocage, and given their proximity to the FOC these sites may be the exit portal and mineralization site.	DISCUSS
+202	210	ferritin	protein_type	The constellation of charged residues on the outer circumference of EncFtn (His57, Glu61 and Glu64) could function in the same way as the residues lining the mineralization surface within the classical ferritin nanocage, and given their proximity to the FOC these sites may be the exit portal and mineralization site.	DISCUSS
+211	219	nanocage	complex_assembly	The constellation of charged residues on the outer circumference of EncFtn (His57, Glu61 and Glu64) could function in the same way as the residues lining the mineralization surface within the classical ferritin nanocage, and given their proximity to the FOC these sites may be the exit portal and mineralization site.	DISCUSS
+254	257	FOC	site	The constellation of charged residues on the outer circumference of EncFtn (His57, Glu61 and Glu64) could function in the same way as the residues lining the mineralization surface within the classical ferritin nanocage, and given their proximity to the FOC these sites may be the exit portal and mineralization site.	DISCUSS
+281	292	exit portal	site	The constellation of charged residues on the outer circumference of EncFtn (His57, Glu61 and Glu64) could function in the same way as the residues lining the mineralization surface within the classical ferritin nanocage, and given their proximity to the FOC these sites may be the exit portal and mineralization site.	DISCUSS
+297	316	mineralization site	site	The constellation of charged residues on the outer circumference of EncFtn (His57, Glu61 and Glu64) could function in the same way as the residues lining the mineralization surface within the classical ferritin nanocage, and given their proximity to the FOC these sites may be the exit portal and mineralization site.	DISCUSS
+87	96	ferritins	protein_type	The absolute requirement for the spatial separation of oxidation and mineralization in ferritins suggests that the EncFtn family proteins are not capable of storing iron minerals due to the absence of an enclosed compartment in their structure (Figure 6—figure supplement 1B).	DISCUSS
+115	121	EncFtn	protein_type	The absolute requirement for the spatial separation of oxidation and mineralization in ferritins suggests that the EncFtn family proteins are not capable of storing iron minerals due to the absence of an enclosed compartment in their structure (Figure 6—figure supplement 1B).	DISCUSS
+165	169	iron	chemical	The absolute requirement for the spatial separation of oxidation and mineralization in ferritins suggests that the EncFtn family proteins are not capable of storing iron minerals due to the absence of an enclosed compartment in their structure (Figure 6—figure supplement 1B).	DISCUSS
+190	200	absence of	protein_state	The absolute requirement for the spatial separation of oxidation and mineralization in ferritins suggests that the EncFtn family proteins are not capable of storing iron minerals due to the absence of an enclosed compartment in their structure (Figure 6—figure supplement 1B).	DISCUSS
+4	32	biochemical characterization	experimental_method	Our biochemical characterization of EncFtn supports this hypothesis, indicating that while this protein is capable of oxidizing iron, it does not accrue mineralized iron in an analogous manner to classical ferritins.	DISCUSS
+36	42	EncFtn	protein	Our biochemical characterization of EncFtn supports this hypothesis, indicating that while this protein is capable of oxidizing iron, it does not accrue mineralized iron in an analogous manner to classical ferritins.	DISCUSS
+128	132	iron	chemical	Our biochemical characterization of EncFtn supports this hypothesis, indicating that while this protein is capable of oxidizing iron, it does not accrue mineralized iron in an analogous manner to classical ferritins.	DISCUSS
+165	169	iron	chemical	Our biochemical characterization of EncFtn supports this hypothesis, indicating that while this protein is capable of oxidizing iron, it does not accrue mineralized iron in an analogous manner to classical ferritins.	DISCUSS
+196	205	classical	protein_state	Our biochemical characterization of EncFtn supports this hypothesis, indicating that while this protein is capable of oxidizing iron, it does not accrue mineralized iron in an analogous manner to classical ferritins.	DISCUSS
+206	215	ferritins	protein_type	Our biochemical characterization of EncFtn supports this hypothesis, indicating that while this protein is capable of oxidizing iron, it does not accrue mineralized iron in an analogous manner to classical ferritins.	DISCUSS
+6	12	EncFtn	protein	While EncFtn does not store iron itself, its association with the encapsulin nanocage suggests that mineralization occurs within the cavity of the encapsulin shell.	DISCUSS
+28	32	iron	chemical	While EncFtn does not store iron itself, its association with the encapsulin nanocage suggests that mineralization occurs within the cavity of the encapsulin shell.	DISCUSS
+66	76	encapsulin	protein	While EncFtn does not store iron itself, its association with the encapsulin nanocage suggests that mineralization occurs within the cavity of the encapsulin shell.	DISCUSS
+77	85	nanocage	complex_assembly	While EncFtn does not store iron itself, its association with the encapsulin nanocage suggests that mineralization occurs within the cavity of the encapsulin shell.	DISCUSS
+133	139	cavity	site	While EncFtn does not store iron itself, its association with the encapsulin nanocage suggests that mineralization occurs within the cavity of the encapsulin shell.	DISCUSS
+147	157	encapsulin	protein	While EncFtn does not store iron itself, its association with the encapsulin nanocage suggests that mineralization occurs within the cavity of the encapsulin shell.	DISCUSS
+158	163	shell	structure_element	While EncFtn does not store iron itself, its association with the encapsulin nanocage suggests that mineralization occurs within the cavity of the encapsulin shell.	DISCUSS
+4	21	ferroxidase assay	experimental_method	Our ferroxidase assay data on the recombinant EncFtn-Enc nanocompartments, which accrue over 4100 iron ions per complex and form regular nanoparticles, are consistent with the encapsulin protein acting as the store for iron oxidized by the EncFtn enzyme.	DISCUSS
+46	56	EncFtn-Enc	complex_assembly	Our ferroxidase assay data on the recombinant EncFtn-Enc nanocompartments, which accrue over 4100 iron ions per complex and form regular nanoparticles, are consistent with the encapsulin protein acting as the store for iron oxidized by the EncFtn enzyme.	DISCUSS
+57	73	nanocompartments	complex_assembly	Our ferroxidase assay data on the recombinant EncFtn-Enc nanocompartments, which accrue over 4100 iron ions per complex and form regular nanoparticles, are consistent with the encapsulin protein acting as the store for iron oxidized by the EncFtn enzyme.	DISCUSS
+98	102	iron	chemical	Our ferroxidase assay data on the recombinant EncFtn-Enc nanocompartments, which accrue over 4100 iron ions per complex and form regular nanoparticles, are consistent with the encapsulin protein acting as the store for iron oxidized by the EncFtn enzyme.	DISCUSS
+137	150	nanoparticles	complex_assembly	Our ferroxidase assay data on the recombinant EncFtn-Enc nanocompartments, which accrue over 4100 iron ions per complex and form regular nanoparticles, are consistent with the encapsulin protein acting as the store for iron oxidized by the EncFtn enzyme.	DISCUSS
+176	186	encapsulin	protein	Our ferroxidase assay data on the recombinant EncFtn-Enc nanocompartments, which accrue over 4100 iron ions per complex and form regular nanoparticles, are consistent with the encapsulin protein acting as the store for iron oxidized by the EncFtn enzyme.	DISCUSS
+219	223	iron	chemical	Our ferroxidase assay data on the recombinant EncFtn-Enc nanocompartments, which accrue over 4100 iron ions per complex and form regular nanoparticles, are consistent with the encapsulin protein acting as the store for iron oxidized by the EncFtn enzyme.	DISCUSS
+240	246	EncFtn	protein	Our ferroxidase assay data on the recombinant EncFtn-Enc nanocompartments, which accrue over 4100 iron ions per complex and form regular nanoparticles, are consistent with the encapsulin protein acting as the store for iron oxidized by the EncFtn enzyme.	DISCUSS
+0	3	TEM	experimental_method	TEM analysis of the reaction products shows the production of homogeneous iron nanoparticles only in the EncFtn-Enc nanocompartment (Figure 8—figure supplement 1).	DISCUSS
+74	78	iron	chemical	TEM analysis of the reaction products shows the production of homogeneous iron nanoparticles only in the EncFtn-Enc nanocompartment (Figure 8—figure supplement 1).	DISCUSS
+105	115	EncFtn-Enc	complex_assembly	TEM analysis of the reaction products shows the production of homogeneous iron nanoparticles only in the EncFtn-Enc nanocompartment (Figure 8—figure supplement 1).	DISCUSS
+116	131	nanocompartment	complex_assembly	TEM analysis of the reaction products shows the production of homogeneous iron nanoparticles only in the EncFtn-Enc nanocompartment (Figure 8—figure supplement 1).	DISCUSS
+9	13	iron	chemical	Model of iron oxidation in encapsulin nanocompartments.	FIG
+27	37	encapsulin	protein	Model of iron oxidation in encapsulin nanocompartments.	FIG
+38	54	nanocompartments	complex_assembly	Model of iron oxidation in encapsulin nanocompartments.	FIG
+13	21	EncFtnsH	protein	(A) Model of EncFtnsH docking to the encapsulin shell.	FIG
+22	29	docking	experimental_method	(A) Model of EncFtnsH docking to the encapsulin shell.	FIG
+37	47	encapsulin	protein	(A) Model of EncFtnsH docking to the encapsulin shell.	FIG
+48	53	shell	structure_element	(A) Model of EncFtnsH docking to the encapsulin shell.	FIG
+9	17	pentamer	oligomeric_state	A single pentamer of the icosahedral T. maritima encapsulin structure (PDBID: 3DKT) is shown as a blue surface with the encapsulin localization sequence of EncFtn shown as a purple surface.	FIG
+25	36	icosahedral	protein_state	A single pentamer of the icosahedral T. maritima encapsulin structure (PDBID: 3DKT) is shown as a blue surface with the encapsulin localization sequence of EncFtn shown as a purple surface.	FIG
+37	48	T. maritima	species	A single pentamer of the icosahedral T. maritima encapsulin structure (PDBID: 3DKT) is shown as a blue surface with the encapsulin localization sequence of EncFtn shown as a purple surface.	FIG
+49	59	encapsulin	protein	A single pentamer of the icosahedral T. maritima encapsulin structure (PDBID: 3DKT) is shown as a blue surface with the encapsulin localization sequence of EncFtn shown as a purple surface.	FIG
+60	69	structure	evidence	A single pentamer of the icosahedral T. maritima encapsulin structure (PDBID: 3DKT) is shown as a blue surface with the encapsulin localization sequence of EncFtn shown as a purple surface.	FIG
+120	130	encapsulin	protein	A single pentamer of the icosahedral T. maritima encapsulin structure (PDBID: 3DKT) is shown as a blue surface with the encapsulin localization sequence of EncFtn shown as a purple surface.	FIG
+131	152	localization sequence	structure_element	A single pentamer of the icosahedral T. maritima encapsulin structure (PDBID: 3DKT) is shown as a blue surface with the encapsulin localization sequence of EncFtn shown as a purple surface.	FIG
+156	162	EncFtn	protein	A single pentamer of the icosahedral T. maritima encapsulin structure (PDBID: 3DKT) is shown as a blue surface with the encapsulin localization sequence of EncFtn shown as a purple surface.	FIG
+30	36	EncFtn	protein	The C-terminal regions of the EncFtn subunits correspond to the position of the localization sequences seen in 3DKT.	FIG
+37	45	subunits	structure_element	The C-terminal regions of the EncFtn subunits correspond to the position of the localization sequences seen in 3DKT.	FIG
+80	102	localization sequences	structure_element	The C-terminal regions of the EncFtn subunits correspond to the position of the localization sequences seen in 3DKT.	FIG
+0	9	Alignment	experimental_method	Alignment of EncFtnsH with 3DKT positions the central channel directly above the pore in the 3DKT pentamer axis (shown as a grey pentagon). (B) Surface view of EncFtn within the encapsulin nanocompartment (grey and blue respectively).	FIG
+13	21	EncFtnsH	protein	Alignment of EncFtnsH with 3DKT positions the central channel directly above the pore in the 3DKT pentamer axis (shown as a grey pentagon). (B) Surface view of EncFtn within the encapsulin nanocompartment (grey and blue respectively).	FIG
+46	61	central channel	site	Alignment of EncFtnsH with 3DKT positions the central channel directly above the pore in the 3DKT pentamer axis (shown as a grey pentagon). (B) Surface view of EncFtn within the encapsulin nanocompartment (grey and blue respectively).	FIG
+81	85	pore	site	Alignment of EncFtnsH with 3DKT positions the central channel directly above the pore in the 3DKT pentamer axis (shown as a grey pentagon). (B) Surface view of EncFtn within the encapsulin nanocompartment (grey and blue respectively).	FIG
+98	106	pentamer	oligomeric_state	Alignment of EncFtnsH with 3DKT positions the central channel directly above the pore in the 3DKT pentamer axis (shown as a grey pentagon). (B) Surface view of EncFtn within the encapsulin nanocompartment (grey and blue respectively).	FIG
+160	166	EncFtn	protein	Alignment of EncFtnsH with 3DKT positions the central channel directly above the pore in the 3DKT pentamer axis (shown as a grey pentagon). (B) Surface view of EncFtn within the encapsulin nanocompartment (grey and blue respectively).	FIG
+178	188	encapsulin	protein	Alignment of EncFtnsH with 3DKT positions the central channel directly above the pore in the 3DKT pentamer axis (shown as a grey pentagon). (B) Surface view of EncFtn within the encapsulin nanocompartment (grey and blue respectively).	FIG
+189	204	nanocompartment	complex_assembly	Alignment of EncFtnsH with 3DKT positions the central channel directly above the pore in the 3DKT pentamer axis (shown as a grey pentagon). (B) Surface view of EncFtn within the encapsulin nanocompartment (grey and blue respectively).	FIG
+17	27	encapsulin	protein	The lumen of the encapsulin nanocompartment is considerably larger than the interior of ferritin (shown in orange behind the encapsulin for reference) and thus allows the storage of significantly more iron.	FIG
+28	43	nanocompartment	complex_assembly	The lumen of the encapsulin nanocompartment is considerably larger than the interior of ferritin (shown in orange behind the encapsulin for reference) and thus allows the storage of significantly more iron.	FIG
+88	96	ferritin	protein_type	The lumen of the encapsulin nanocompartment is considerably larger than the interior of ferritin (shown in orange behind the encapsulin for reference) and thus allows the storage of significantly more iron.	FIG
+125	135	encapsulin	protein	The lumen of the encapsulin nanocompartment is considerably larger than the interior of ferritin (shown in orange behind the encapsulin for reference) and thus allows the storage of significantly more iron.	FIG
+201	205	iron	chemical	The lumen of the encapsulin nanocompartment is considerably larger than the interior of ferritin (shown in orange behind the encapsulin for reference) and thus allows the storage of significantly more iron.	FIG
+25	29	iron	chemical	The proposed pathway for iron movement through the encapsulin shell and EncFtn FOC is shown with arrows. (C) Model ofiron oxidation within an encapsulin nanocompartment.	FIG
+51	61	encapsulin	protein	The proposed pathway for iron movement through the encapsulin shell and EncFtn FOC is shown with arrows. (C) Model ofiron oxidation within an encapsulin nanocompartment.	FIG
+62	67	shell	structure_element	The proposed pathway for iron movement through the encapsulin shell and EncFtn FOC is shown with arrows. (C) Model ofiron oxidation within an encapsulin nanocompartment.	FIG
+72	78	EncFtn	protein	The proposed pathway for iron movement through the encapsulin shell and EncFtn FOC is shown with arrows. (C) Model ofiron oxidation within an encapsulin nanocompartment.	FIG
+79	82	FOC	site	The proposed pathway for iron movement through the encapsulin shell and EncFtn FOC is shown with arrows. (C) Model ofiron oxidation within an encapsulin nanocompartment.	FIG
+142	152	encapsulin	protein	The proposed pathway for iron movement through the encapsulin shell and EncFtn FOC is shown with arrows. (C) Model ofiron oxidation within an encapsulin nanocompartment.	FIG
+153	168	nanocompartment	complex_assembly	The proposed pathway for iron movement through the encapsulin shell and EncFtn FOC is shown with arrows. (C) Model ofiron oxidation within an encapsulin nanocompartment.	FIG
+3	9	EncFtn	protein	As EncFtn is unable to mineralize iron on its surface directly, Fe2+ must pass through the encapsulin shell to access the first metal binding site within the central channel of EncFtnsH (entry site) prior to oxidation within the FOC and release as Fe3+ to the outer surface of the protein where it can be mineralized within the lumen of the encapsulin cage.	FIG
+34	38	iron	chemical	As EncFtn is unable to mineralize iron on its surface directly, Fe2+ must pass through the encapsulin shell to access the first metal binding site within the central channel of EncFtnsH (entry site) prior to oxidation within the FOC and release as Fe3+ to the outer surface of the protein where it can be mineralized within the lumen of the encapsulin cage.	FIG
+64	68	Fe2+	chemical	As EncFtn is unable to mineralize iron on its surface directly, Fe2+ must pass through the encapsulin shell to access the first metal binding site within the central channel of EncFtnsH (entry site) prior to oxidation within the FOC and release as Fe3+ to the outer surface of the protein where it can be mineralized within the lumen of the encapsulin cage.	FIG
+91	101	encapsulin	protein	As EncFtn is unable to mineralize iron on its surface directly, Fe2+ must pass through the encapsulin shell to access the first metal binding site within the central channel of EncFtnsH (entry site) prior to oxidation within the FOC and release as Fe3+ to the outer surface of the protein where it can be mineralized within the lumen of the encapsulin cage.	FIG
+102	107	shell	structure_element	As EncFtn is unable to mineralize iron on its surface directly, Fe2+ must pass through the encapsulin shell to access the first metal binding site within the central channel of EncFtnsH (entry site) prior to oxidation within the FOC and release as Fe3+ to the outer surface of the protein where it can be mineralized within the lumen of the encapsulin cage.	FIG
+128	146	metal binding site	site	As EncFtn is unable to mineralize iron on its surface directly, Fe2+ must pass through the encapsulin shell to access the first metal binding site within the central channel of EncFtnsH (entry site) prior to oxidation within the FOC and release as Fe3+ to the outer surface of the protein where it can be mineralized within the lumen of the encapsulin cage.	FIG
+158	173	central channel	site	As EncFtn is unable to mineralize iron on its surface directly, Fe2+ must pass through the encapsulin shell to access the first metal binding site within the central channel of EncFtnsH (entry site) prior to oxidation within the FOC and release as Fe3+ to the outer surface of the protein where it can be mineralized within the lumen of the encapsulin cage.	FIG
+177	185	EncFtnsH	protein	As EncFtn is unable to mineralize iron on its surface directly, Fe2+ must pass through the encapsulin shell to access the first metal binding site within the central channel of EncFtnsH (entry site) prior to oxidation within the FOC and release as Fe3+ to the outer surface of the protein where it can be mineralized within the lumen of the encapsulin cage.	FIG
+187	197	entry site	site	As EncFtn is unable to mineralize iron on its surface directly, Fe2+ must pass through the encapsulin shell to access the first metal binding site within the central channel of EncFtnsH (entry site) prior to oxidation within the FOC and release as Fe3+ to the outer surface of the protein where it can be mineralized within the lumen of the encapsulin cage.	FIG
+229	232	FOC	site	As EncFtn is unable to mineralize iron on its surface directly, Fe2+ must pass through the encapsulin shell to access the first metal binding site within the central channel of EncFtnsH (entry site) prior to oxidation within the FOC and release as Fe3+ to the outer surface of the protein where it can be mineralized within the lumen of the encapsulin cage.	FIG
+248	252	Fe3+	chemical	As EncFtn is unable to mineralize iron on its surface directly, Fe2+ must pass through the encapsulin shell to access the first metal binding site within the central channel of EncFtnsH (entry site) prior to oxidation within the FOC and release as Fe3+ to the outer surface of the protein where it can be mineralized within the lumen of the encapsulin cage.	FIG
+341	351	encapsulin	protein	As EncFtn is unable to mineralize iron on its surface directly, Fe2+ must pass through the encapsulin shell to access the first metal binding site within the central channel of EncFtnsH (entry site) prior to oxidation within the FOC and release as Fe3+ to the outer surface of the protein where it can be mineralized within the lumen of the encapsulin cage.	FIG
+0	7	Docking	experimental_method	Docking the decamer structure of EncFtnsH into the pentamer of the T. maritima encapsulin Tmari_0786 (PDB ID: 3DKT)  shows that the position of the C-terminal extensions of our EncFtnsH structure are consistent with the localization sequences seen bound to the encapsulin protein (Figure 14A).	DISCUSS
+12	19	decamer	oligomeric_state	Docking the decamer structure of EncFtnsH into the pentamer of the T. maritima encapsulin Tmari_0786 (PDB ID: 3DKT)  shows that the position of the C-terminal extensions of our EncFtnsH structure are consistent with the localization sequences seen bound to the encapsulin protein (Figure 14A).	DISCUSS
+20	29	structure	evidence	Docking the decamer structure of EncFtnsH into the pentamer of the T. maritima encapsulin Tmari_0786 (PDB ID: 3DKT)  shows that the position of the C-terminal extensions of our EncFtnsH structure are consistent with the localization sequences seen bound to the encapsulin protein (Figure 14A).	DISCUSS
+33	41	EncFtnsH	protein	Docking the decamer structure of EncFtnsH into the pentamer of the T. maritima encapsulin Tmari_0786 (PDB ID: 3DKT)  shows that the position of the C-terminal extensions of our EncFtnsH structure are consistent with the localization sequences seen bound to the encapsulin protein (Figure 14A).	DISCUSS
+51	59	pentamer	oligomeric_state	Docking the decamer structure of EncFtnsH into the pentamer of the T. maritima encapsulin Tmari_0786 (PDB ID: 3DKT)  shows that the position of the C-terminal extensions of our EncFtnsH structure are consistent with the localization sequences seen bound to the encapsulin protein (Figure 14A).	DISCUSS
+67	78	T. maritima	species	Docking the decamer structure of EncFtnsH into the pentamer of the T. maritima encapsulin Tmari_0786 (PDB ID: 3DKT)  shows that the position of the C-terminal extensions of our EncFtnsH structure are consistent with the localization sequences seen bound to the encapsulin protein (Figure 14A).	DISCUSS
+79	89	encapsulin	protein	Docking the decamer structure of EncFtnsH into the pentamer of the T. maritima encapsulin Tmari_0786 (PDB ID: 3DKT)  shows that the position of the C-terminal extensions of our EncFtnsH structure are consistent with the localization sequences seen bound to the encapsulin protein (Figure 14A).	DISCUSS
+90	100	Tmari_0786	gene	Docking the decamer structure of EncFtnsH into the pentamer of the T. maritima encapsulin Tmari_0786 (PDB ID: 3DKT)  shows that the position of the C-terminal extensions of our EncFtnsH structure are consistent with the localization sequences seen bound to the encapsulin protein (Figure 14A).	DISCUSS
+148	169	C-terminal extensions	structure_element	Docking the decamer structure of EncFtnsH into the pentamer of the T. maritima encapsulin Tmari_0786 (PDB ID: 3DKT)  shows that the position of the C-terminal extensions of our EncFtnsH structure are consistent with the localization sequences seen bound to the encapsulin protein (Figure 14A).	DISCUSS
+177	185	EncFtnsH	protein	Docking the decamer structure of EncFtnsH into the pentamer of the T. maritima encapsulin Tmari_0786 (PDB ID: 3DKT)  shows that the position of the C-terminal extensions of our EncFtnsH structure are consistent with the localization sequences seen bound to the encapsulin protein (Figure 14A).	DISCUSS
+186	195	structure	evidence	Docking the decamer structure of EncFtnsH into the pentamer of the T. maritima encapsulin Tmari_0786 (PDB ID: 3DKT)  shows that the position of the C-terminal extensions of our EncFtnsH structure are consistent with the localization sequences seen bound to the encapsulin protein (Figure 14A).	DISCUSS
+220	242	localization sequences	structure_element	Docking the decamer structure of EncFtnsH into the pentamer of the T. maritima encapsulin Tmari_0786 (PDB ID: 3DKT)  shows that the position of the C-terminal extensions of our EncFtnsH structure are consistent with the localization sequences seen bound to the encapsulin protein (Figure 14A).	DISCUSS
+248	256	bound to	protein_state	Docking the decamer structure of EncFtnsH into the pentamer of the T. maritima encapsulin Tmari_0786 (PDB ID: 3DKT)  shows that the position of the C-terminal extensions of our EncFtnsH structure are consistent with the localization sequences seen bound to the encapsulin protein (Figure 14A).	DISCUSS
+261	271	encapsulin	protein	Docking the decamer structure of EncFtnsH into the pentamer of the T. maritima encapsulin Tmari_0786 (PDB ID: 3DKT)  shows that the position of the C-terminal extensions of our EncFtnsH structure are consistent with the localization sequences seen bound to the encapsulin protein (Figure 14A).	DISCUSS
+26	32	EncFtn	protein	Thus, it appears that the EncFtn decamer is the physiological state of this protein.	DISCUSS
+33	40	decamer	oligomeric_state	Thus, it appears that the EncFtn decamer is the physiological state of this protein.	DISCUSS
+31	43	central ring	structure_element	This arrangement positions the central ring of EncFtn directly above the pore at the five-fold symmetry axis of the encapsulin shell and highlights a potential route for the entry of iron into the encapsulin and towards the active site of EncFtn.	DISCUSS
+47	53	EncFtn	protein	This arrangement positions the central ring of EncFtn directly above the pore at the five-fold symmetry axis of the encapsulin shell and highlights a potential route for the entry of iron into the encapsulin and towards the active site of EncFtn.	DISCUSS
+73	77	pore	site	This arrangement positions the central ring of EncFtn directly above the pore at the five-fold symmetry axis of the encapsulin shell and highlights a potential route for the entry of iron into the encapsulin and towards the active site of EncFtn.	DISCUSS
+116	126	encapsulin	protein	This arrangement positions the central ring of EncFtn directly above the pore at the five-fold symmetry axis of the encapsulin shell and highlights a potential route for the entry of iron into the encapsulin and towards the active site of EncFtn.	DISCUSS
+127	132	shell	structure_element	This arrangement positions the central ring of EncFtn directly above the pore at the five-fold symmetry axis of the encapsulin shell and highlights a potential route for the entry of iron into the encapsulin and towards the active site of EncFtn.	DISCUSS
+183	187	iron	chemical	This arrangement positions the central ring of EncFtn directly above the pore at the five-fold symmetry axis of the encapsulin shell and highlights a potential route for the entry of iron into the encapsulin and towards the active site of EncFtn.	DISCUSS
+197	207	encapsulin	protein	This arrangement positions the central ring of EncFtn directly above the pore at the five-fold symmetry axis of the encapsulin shell and highlights a potential route for the entry of iron into the encapsulin and towards the active site of EncFtn.	DISCUSS
+224	235	active site	site	This arrangement positions the central ring of EncFtn directly above the pore at the five-fold symmetry axis of the encapsulin shell and highlights a potential route for the entry of iron into the encapsulin and towards the active site of EncFtn.	DISCUSS
+239	245	EncFtn	protein	This arrangement positions the central ring of EncFtn directly above the pore at the five-fold symmetry axis of the encapsulin shell and highlights a potential route for the entry of iron into the encapsulin and towards the active site of EncFtn.	DISCUSS
+20	30	encapsulin	protein	A comparison of the encapsulin nanocompartment and the ferritin nanocage highlights the size differential between the two complexes (Figure 14B) that allows the encapsulin to store significantly more iron.	DISCUSS
+31	46	nanocompartment	complex_assembly	A comparison of the encapsulin nanocompartment and the ferritin nanocage highlights the size differential between the two complexes (Figure 14B) that allows the encapsulin to store significantly more iron.	DISCUSS
+55	63	ferritin	protein_type	A comparison of the encapsulin nanocompartment and the ferritin nanocage highlights the size differential between the two complexes (Figure 14B) that allows the encapsulin to store significantly more iron.	DISCUSS
+64	72	nanocage	complex_assembly	A comparison of the encapsulin nanocompartment and the ferritin nanocage highlights the size differential between the two complexes (Figure 14B) that allows the encapsulin to store significantly more iron.	DISCUSS
+161	171	encapsulin	protein	A comparison of the encapsulin nanocompartment and the ferritin nanocage highlights the size differential between the two complexes (Figure 14B) that allows the encapsulin to store significantly more iron.	DISCUSS
+200	204	iron	chemical	A comparison of the encapsulin nanocompartment and the ferritin nanocage highlights the size differential between the two complexes (Figure 14B) that allows the encapsulin to store significantly more iron.	DISCUSS
+4	15	presence of	protein_state	The presence of five FOCs per EncFtnsH decamer and the fact that the icosahedral encapsulin nanocage can hold up to twelve of decameric EncFtn between each of the internal five-fold vertices means that they can achieve a high rate of iron mineralization across the entire nanocompartment.	DISCUSS
+21	25	FOCs	site	The presence of five FOCs per EncFtnsH decamer and the fact that the icosahedral encapsulin nanocage can hold up to twelve of decameric EncFtn between each of the internal five-fold vertices means that they can achieve a high rate of iron mineralization across the entire nanocompartment.	DISCUSS
+30	38	EncFtnsH	protein	The presence of five FOCs per EncFtnsH decamer and the fact that the icosahedral encapsulin nanocage can hold up to twelve of decameric EncFtn between each of the internal five-fold vertices means that they can achieve a high rate of iron mineralization across the entire nanocompartment.	DISCUSS
+39	46	decamer	oligomeric_state	The presence of five FOCs per EncFtnsH decamer and the fact that the icosahedral encapsulin nanocage can hold up to twelve of decameric EncFtn between each of the internal five-fold vertices means that they can achieve a high rate of iron mineralization across the entire nanocompartment.	DISCUSS
+69	80	icosahedral	protein_state	The presence of five FOCs per EncFtnsH decamer and the fact that the icosahedral encapsulin nanocage can hold up to twelve of decameric EncFtn between each of the internal five-fold vertices means that they can achieve a high rate of iron mineralization across the entire nanocompartment.	DISCUSS
+81	91	encapsulin	protein	The presence of five FOCs per EncFtnsH decamer and the fact that the icosahedral encapsulin nanocage can hold up to twelve of decameric EncFtn between each of the internal five-fold vertices means that they can achieve a high rate of iron mineralization across the entire nanocompartment.	DISCUSS
+92	100	nanocage	complex_assembly	The presence of five FOCs per EncFtnsH decamer and the fact that the icosahedral encapsulin nanocage can hold up to twelve of decameric EncFtn between each of the internal five-fold vertices means that they can achieve a high rate of iron mineralization across the entire nanocompartment.	DISCUSS
+126	135	decameric	oligomeric_state	The presence of five FOCs per EncFtnsH decamer and the fact that the icosahedral encapsulin nanocage can hold up to twelve of decameric EncFtn between each of the internal five-fold vertices means that they can achieve a high rate of iron mineralization across the entire nanocompartment.	DISCUSS
+136	142	EncFtn	protein	The presence of five FOCs per EncFtnsH decamer and the fact that the icosahedral encapsulin nanocage can hold up to twelve of decameric EncFtn between each of the internal five-fold vertices means that they can achieve a high rate of iron mineralization across the entire nanocompartment.	DISCUSS
+234	238	iron	chemical	The presence of five FOCs per EncFtnsH decamer and the fact that the icosahedral encapsulin nanocage can hold up to twelve of decameric EncFtn between each of the internal five-fold vertices means that they can achieve a high rate of iron mineralization across the entire nanocompartment.	DISCUSS
+272	287	nanocompartment	complex_assembly	The presence of five FOCs per EncFtnsH decamer and the fact that the icosahedral encapsulin nanocage can hold up to twelve of decameric EncFtn between each of the internal five-fold vertices means that they can achieve a high rate of iron mineralization across the entire nanocompartment.	DISCUSS
+93	102	classical	protein_state	This arrangement of multiple reaction centers in a single protein assembly is reminiscent of classical ferritins, which has 24 FOCs distributed around the nanocage.	DISCUSS
+103	112	ferritins	protein_type	This arrangement of multiple reaction centers in a single protein assembly is reminiscent of classical ferritins, which has 24 FOCs distributed around the nanocage.	DISCUSS
+127	131	FOCs	site	This arrangement of multiple reaction centers in a single protein assembly is reminiscent of classical ferritins, which has 24 FOCs distributed around the nanocage.	DISCUSS
+155	163	nanocage	complex_assembly	This arrangement of multiple reaction centers in a single protein assembly is reminiscent of classical ferritins, which has 24 FOCs distributed around the nanocage.	DISCUSS
+4	19	structural data	evidence	Our structural data, coupled with biochemical and ICP-MS analysis, suggest a model for the activity of the encapsulin iron-megastore (Figure 14C).	DISCUSS
+34	56	biochemical and ICP-MS	experimental_method	Our structural data, coupled with biochemical and ICP-MS analysis, suggest a model for the activity of the encapsulin iron-megastore (Figure 14C).	DISCUSS
+107	117	encapsulin	protein	Our structural data, coupled with biochemical and ICP-MS analysis, suggest a model for the activity of the encapsulin iron-megastore (Figure 14C).	DISCUSS
+118	132	iron-megastore	complex_assembly	Our structural data, coupled with biochemical and ICP-MS analysis, suggest a model for the activity of the encapsulin iron-megastore (Figure 14C).	DISCUSS
+4	21	crystal structure	evidence	The crystal structure of the T. maritima encapsulin shell protein has a negatively charged pore positioned to allow the passage of Fe2+ into the encapsulin and directs the metal towards the central, negatively charged hole of the EncFtn ring (Figure 4—figure supplement 1).	DISCUSS
+29	40	T. maritima	species	The crystal structure of the T. maritima encapsulin shell protein has a negatively charged pore positioned to allow the passage of Fe2+ into the encapsulin and directs the metal towards the central, negatively charged hole of the EncFtn ring (Figure 4—figure supplement 1).	DISCUSS
+41	51	encapsulin	protein	The crystal structure of the T. maritima encapsulin shell protein has a negatively charged pore positioned to allow the passage of Fe2+ into the encapsulin and directs the metal towards the central, negatively charged hole of the EncFtn ring (Figure 4—figure supplement 1).	DISCUSS
+52	57	shell	structure_element	The crystal structure of the T. maritima encapsulin shell protein has a negatively charged pore positioned to allow the passage of Fe2+ into the encapsulin and directs the metal towards the central, negatively charged hole of the EncFtn ring (Figure 4—figure supplement 1).	DISCUSS
+72	95	negatively charged pore	site	The crystal structure of the T. maritima encapsulin shell protein has a negatively charged pore positioned to allow the passage of Fe2+ into the encapsulin and directs the metal towards the central, negatively charged hole of the EncFtn ring (Figure 4—figure supplement 1).	DISCUSS
+131	135	Fe2+	chemical	The crystal structure of the T. maritima encapsulin shell protein has a negatively charged pore positioned to allow the passage of Fe2+ into the encapsulin and directs the metal towards the central, negatively charged hole of the EncFtn ring (Figure 4—figure supplement 1).	DISCUSS
+145	155	encapsulin	protein	The crystal structure of the T. maritima encapsulin shell protein has a negatively charged pore positioned to allow the passage of Fe2+ into the encapsulin and directs the metal towards the central, negatively charged hole of the EncFtn ring (Figure 4—figure supplement 1).	DISCUSS
+199	222	negatively charged hole	site	The crystal structure of the T. maritima encapsulin shell protein has a negatively charged pore positioned to allow the passage of Fe2+ into the encapsulin and directs the metal towards the central, negatively charged hole of the EncFtn ring (Figure 4—figure supplement 1).	DISCUSS
+230	236	EncFtn	protein	The crystal structure of the T. maritima encapsulin shell protein has a negatively charged pore positioned to allow the passage of Fe2+ into the encapsulin and directs the metal towards the central, negatively charged hole of the EncFtn ring (Figure 4—figure supplement 1).	DISCUSS
+237	241	ring	structure_element	The crystal structure of the T. maritima encapsulin shell protein has a negatively charged pore positioned to allow the passage of Fe2+ into the encapsulin and directs the metal towards the central, negatively charged hole of the EncFtn ring (Figure 4—figure supplement 1).	DISCUSS
+9	28	metal-binding sites	site	The five metal-binding sites on the interior of the ring (Glu31/34-sites) may select for the Fe2+ ion and direct it towards their cognate FOCs.	DISCUSS
+52	56	ring	structure_element	The five metal-binding sites on the interior of the ring (Glu31/34-sites) may select for the Fe2+ ion and direct it towards their cognate FOCs.	DISCUSS
+58	72	Glu31/34-sites	site	The five metal-binding sites on the interior of the ring (Glu31/34-sites) may select for the Fe2+ ion and direct it towards their cognate FOCs.	DISCUSS
+93	97	Fe2+	chemical	The five metal-binding sites on the interior of the ring (Glu31/34-sites) may select for the Fe2+ ion and direct it towards their cognate FOCs.	DISCUSS
+138	142	FOCs	site	The five metal-binding sites on the interior of the ring (Glu31/34-sites) may select for the Fe2+ ion and direct it towards their cognate FOCs.	DISCUSS
+33	37	Fe2+	chemical	We propose that the oxidation of Fe2+ to Fe3+ occurs within the FOC according to the model postulated by  in which the FOC acts as a substrate site through which iron passes and is released on to weakly coordinating sites at the outer circumference of the protein (His57, Glu61 and Glu64), where it is able to form ferrihydrite minerals which can be safely deposited within the lumen of the encapsulin nanocompartment (Figure 14).	DISCUSS
+41	45	Fe3+	chemical	We propose that the oxidation of Fe2+ to Fe3+ occurs within the FOC according to the model postulated by  in which the FOC acts as a substrate site through which iron passes and is released on to weakly coordinating sites at the outer circumference of the protein (His57, Glu61 and Glu64), where it is able to form ferrihydrite minerals which can be safely deposited within the lumen of the encapsulin nanocompartment (Figure 14).	DISCUSS
+64	67	FOC	site	We propose that the oxidation of Fe2+ to Fe3+ occurs within the FOC according to the model postulated by  in which the FOC acts as a substrate site through which iron passes and is released on to weakly coordinating sites at the outer circumference of the protein (His57, Glu61 and Glu64), where it is able to form ferrihydrite minerals which can be safely deposited within the lumen of the encapsulin nanocompartment (Figure 14).	DISCUSS
+119	122	FOC	site	We propose that the oxidation of Fe2+ to Fe3+ occurs within the FOC according to the model postulated by  in which the FOC acts as a substrate site through which iron passes and is released on to weakly coordinating sites at the outer circumference of the protein (His57, Glu61 and Glu64), where it is able to form ferrihydrite minerals which can be safely deposited within the lumen of the encapsulin nanocompartment (Figure 14).	DISCUSS
+133	147	substrate site	site	We propose that the oxidation of Fe2+ to Fe3+ occurs within the FOC according to the model postulated by  in which the FOC acts as a substrate site through which iron passes and is released on to weakly coordinating sites at the outer circumference of the protein (His57, Glu61 and Glu64), where it is able to form ferrihydrite minerals which can be safely deposited within the lumen of the encapsulin nanocompartment (Figure 14).	DISCUSS
+162	166	iron	chemical	We propose that the oxidation of Fe2+ to Fe3+ occurs within the FOC according to the model postulated by  in which the FOC acts as a substrate site through which iron passes and is released on to weakly coordinating sites at the outer circumference of the protein (His57, Glu61 and Glu64), where it is able to form ferrihydrite minerals which can be safely deposited within the lumen of the encapsulin nanocompartment (Figure 14).	DISCUSS
+196	221	weakly coordinating sites	site	We propose that the oxidation of Fe2+ to Fe3+ occurs within the FOC according to the model postulated by  in which the FOC acts as a substrate site through which iron passes and is released on to weakly coordinating sites at the outer circumference of the protein (His57, Glu61 and Glu64), where it is able to form ferrihydrite minerals which can be safely deposited within the lumen of the encapsulin nanocompartment (Figure 14).	DISCUSS
+265	270	His57	residue_name_number	We propose that the oxidation of Fe2+ to Fe3+ occurs within the FOC according to the model postulated by  in which the FOC acts as a substrate site through which iron passes and is released on to weakly coordinating sites at the outer circumference of the protein (His57, Glu61 and Glu64), where it is able to form ferrihydrite minerals which can be safely deposited within the lumen of the encapsulin nanocompartment (Figure 14).	DISCUSS
+272	277	Glu61	residue_name_number	We propose that the oxidation of Fe2+ to Fe3+ occurs within the FOC according to the model postulated by  in which the FOC acts as a substrate site through which iron passes and is released on to weakly coordinating sites at the outer circumference of the protein (His57, Glu61 and Glu64), where it is able to form ferrihydrite minerals which can be safely deposited within the lumen of the encapsulin nanocompartment (Figure 14).	DISCUSS
+282	287	Glu64	residue_name_number	We propose that the oxidation of Fe2+ to Fe3+ occurs within the FOC according to the model postulated by  in which the FOC acts as a substrate site through which iron passes and is released on to weakly coordinating sites at the outer circumference of the protein (His57, Glu61 and Glu64), where it is able to form ferrihydrite minerals which can be safely deposited within the lumen of the encapsulin nanocompartment (Figure 14).	DISCUSS
+315	327	ferrihydrite	chemical	We propose that the oxidation of Fe2+ to Fe3+ occurs within the FOC according to the model postulated by  in which the FOC acts as a substrate site through which iron passes and is released on to weakly coordinating sites at the outer circumference of the protein (His57, Glu61 and Glu64), where it is able to form ferrihydrite minerals which can be safely deposited within the lumen of the encapsulin nanocompartment (Figure 14).	DISCUSS
+391	401	encapsulin	protein	We propose that the oxidation of Fe2+ to Fe3+ occurs within the FOC according to the model postulated by  in which the FOC acts as a substrate site through which iron passes and is released on to weakly coordinating sites at the outer circumference of the protein (His57, Glu61 and Glu64), where it is able to form ferrihydrite minerals which can be safely deposited within the lumen of the encapsulin nanocompartment (Figure 14).	DISCUSS
+402	417	nanocompartment	complex_assembly	We propose that the oxidation of Fe2+ to Fe3+ occurs within the FOC according to the model postulated by  in which the FOC acts as a substrate site through which iron passes and is released on to weakly coordinating sites at the outer circumference of the protein (His57, Glu61 and Glu64), where it is able to form ferrihydrite minerals which can be safely deposited within the lumen of the encapsulin nanocompartment (Figure 14).	DISCUSS
+40	49	structure	evidence	Here we describe for the first time the structure and biochemistry of a new class of encapsulin-associated ferritin-like protein and demonstrate that it has an absolute requirement for compartmentalization within an encapsulin nanocage to act as an iron store.	DISCUSS
+85	128	encapsulin-associated ferritin-like protein	protein_type	Here we describe for the first time the structure and biochemistry of a new class of encapsulin-associated ferritin-like protein and demonstrate that it has an absolute requirement for compartmentalization within an encapsulin nanocage to act as an iron store.	DISCUSS
+216	226	encapsulin	protein	Here we describe for the first time the structure and biochemistry of a new class of encapsulin-associated ferritin-like protein and demonstrate that it has an absolute requirement for compartmentalization within an encapsulin nanocage to act as an iron store.	DISCUSS
+227	235	nanocage	complex_assembly	Here we describe for the first time the structure and biochemistry of a new class of encapsulin-associated ferritin-like protein and demonstrate that it has an absolute requirement for compartmentalization within an encapsulin nanocage to act as an iron store.	DISCUSS
+249	253	iron	chemical	Here we describe for the first time the structure and biochemistry of a new class of encapsulin-associated ferritin-like protein and demonstrate that it has an absolute requirement for compartmentalization within an encapsulin nanocage to act as an iron store.	DISCUSS
+20	30	EncFtn-Enc	complex_assembly	Further work on the EncFtn-Enc nanocompartment will establish the structural basis for the movement of iron through the encapsulin shell, the mechanism of iron oxidation by the EncFtn FOC and its subsequent storage in the lumen of the encapsulin nanocompartment.	DISCUSS
+31	46	nanocompartment	complex_assembly	Further work on the EncFtn-Enc nanocompartment will establish the structural basis for the movement of iron through the encapsulin shell, the mechanism of iron oxidation by the EncFtn FOC and its subsequent storage in the lumen of the encapsulin nanocompartment.	DISCUSS
+103	107	iron	chemical	Further work on the EncFtn-Enc nanocompartment will establish the structural basis for the movement of iron through the encapsulin shell, the mechanism of iron oxidation by the EncFtn FOC and its subsequent storage in the lumen of the encapsulin nanocompartment.	DISCUSS
+120	130	encapsulin	protein	Further work on the EncFtn-Enc nanocompartment will establish the structural basis for the movement of iron through the encapsulin shell, the mechanism of iron oxidation by the EncFtn FOC and its subsequent storage in the lumen of the encapsulin nanocompartment.	DISCUSS
+131	136	shell	structure_element	Further work on the EncFtn-Enc nanocompartment will establish the structural basis for the movement of iron through the encapsulin shell, the mechanism of iron oxidation by the EncFtn FOC and its subsequent storage in the lumen of the encapsulin nanocompartment.	DISCUSS
+155	159	iron	chemical	Further work on the EncFtn-Enc nanocompartment will establish the structural basis for the movement of iron through the encapsulin shell, the mechanism of iron oxidation by the EncFtn FOC and its subsequent storage in the lumen of the encapsulin nanocompartment.	DISCUSS
+177	183	EncFtn	protein	Further work on the EncFtn-Enc nanocompartment will establish the structural basis for the movement of iron through the encapsulin shell, the mechanism of iron oxidation by the EncFtn FOC and its subsequent storage in the lumen of the encapsulin nanocompartment.	DISCUSS
+184	187	FOC	site	Further work on the EncFtn-Enc nanocompartment will establish the structural basis for the movement of iron through the encapsulin shell, the mechanism of iron oxidation by the EncFtn FOC and its subsequent storage in the lumen of the encapsulin nanocompartment.	DISCUSS
+235	245	encapsulin	protein	Further work on the EncFtn-Enc nanocompartment will establish the structural basis for the movement of iron through the encapsulin shell, the mechanism of iron oxidation by the EncFtn FOC and its subsequent storage in the lumen of the encapsulin nanocompartment.	DISCUSS
+246	261	nanocompartment	complex_assembly	Further work on the EncFtn-Enc nanocompartment will establish the structural basis for the movement of iron through the encapsulin shell, the mechanism of iron oxidation by the EncFtn FOC and its subsequent storage in the lumen of the encapsulin nanocompartment.	DISCUSS
+77	88	apoferritin	protein_state	TEM imaging was performed on purified encapsulin, EncFtn, and EncFtn-Enc and apoferritin.	METHODS
+129	140	apoferritin	protein_state	To observe iron mineral formation by TEM, protein samples at 8.5 µM concentration including EncFtnsH, encapsulin, EncFtn-Enc and apoferritin were supplemented with acidic Fe(NH4)2(SO4)2 at their maximum iron loading ratio in room temperature for 1 hr.	METHODS
+13	24	apoferritin	protein_state	Horse spleen apoferritin preparation	METHODS
+13	24	apoferritin	protein_state	Horse spleen apoferritin purchased from Sigma Aldrich (UK) was dissolved in deaerated MOPS buffer (100 mM MOPS, 100 mM NaCl, 3 g/100 ml Na2S2O4 and 0.5 M EDTA, pH 6.5).	METHODS
+14	25	apoferritin	protein_state	Fe content of apoferritin was detected using ferrozine assay.	METHODS
+0	11	Apoferritin	protein_state	Apoferritin containing less than 0.5 Fe per 24-mer was used in the ferroxidase assay.	METHODS
+0	11	Apoferritin	protein_state	Apoferritin used in the Fe loading capacity experiment was prepared in the same way with 5–15 Fe per 24-mer.	METHODS
+137	148	apoferritin	protein_state	In order to determine the maximum iron loading capacity, around 8.5 µM proteins including decameric EncFtnsH, Encapsulin, EncFtn-Enc and apoferritin were loaded with various amount of acidic Fe(NH4)2(SO4)2 ranging from 0 to 1700 µM. Protein mixtures were incubated in room temperature for 3 hrs before desalting in Zebra spin desalting columns (7 kDa cut-off, Thermo Fisher Scientific, UK) to remove free iron ions.	METHODS
+180	190	absence of	protein_state	Both monomer and decamer fractions of EncFtnsH left at room temperature for 2 hrs, or overnight, were also analysed as controls to show the stability of the protein samples in the absence of additional metal ions.	METHODS
+49	64	nanocompartment	complex_assembly	Characterization of a Mycobacterium tuberculosis nanocompartment and its potential cargo proteins	REF
+20	35	nanocompartment	complex_assembly	A virus capsid-like nanocompartment that stores iron and protects bacteria from oxidative stress	REF
+48	63	nanocompartment	complex_assembly	Self-sorting of foreign proteins in a bacterial nanocompartment	REF
+58	73	nanocompartment	complex_assembly	Structural basis of enzyme encapsulation into a bacterial nanocompartment	REF
+256	262	oxygen	chemical	1) Methods: What procedures and analyses did the author use to assess whether the iron added to the various ferritin derivatives was protein coated or was simply balls of rust attached to protein fragments? If the latter, it could easily generate reactive oxygen species in air under physiological conditions.	REVIEW_INFO
+109	120	apoferritin	protein_state	Even an experimental situation: 24 subunit (monomer) ferritin with a biomineral prepared experimentally from apoferritin and containing, on average, only 1000 iron atoms/24 subunit cage, the equivalent parameter appears to be 1000/24 = 42.	REVIEW_INFO
+109	120	apoferritin	protein_state	Even an experimental situation: 24 subunit (monomer) ferritin with a biomineral prepared experimentally from apoferritin and containing, on average, only 1000 iron atoms/24 subunit cage, the equivalent parameter appears to be 1000/24 = 42.	REVIEW_INFO
+67	78	apoferritin	protein_state	Missing are data for the starting material, 24 subunit ferritin or apoferritin (ferritin with the iron removed, by reduction and chelation, as a control.)	REVIEW_INFO
+67	78	apoferritin	protein_state	Missing are data for the starting material, 24 subunit ferritin or apoferritin (ferritin with the iron removed, by reduction and chelation, as a control.)	REVIEW_INFO
+34	45	mutagenesis	experimental_method	4) I would have liked to see some mutagenesis experiments to test the models of assembly, iron binding and ferroxidase activity.	REVIEW_INFO
+107	118	ferroxidase	protein_type	4) I would have liked to see some mutagenesis experiments to test the models of assembly, iron binding and ferroxidase activity.	REVIEW_INFO
+44	55	apoferritin	protein_state	These results show the production of ROS by apoferritin, which is consistent with the published data on the reaction mechanism of certain ferritins; however, no significant ROS were detected for the EncFtn or encapsulin proteins.	REVIEW_INFO
+103	118	nanocompartment	complex_assembly	We have clarified this key difference in the discussion of the iron storage function of the encapsulin nanocompartment (subsection “Iron storage in encapsulin nanocompartments”, second paragraph).	REVIEW_INFO
+160	175	nanocompartment	complex_assembly	The key conclusion of the paper is that the iron storage and iron oxidation functions that are combined in classical ferritins are split between the encapsulin nanocompartment and the EncFtn protein.	REVIEW_INFO
+17	28	apoferritin	protein_state	Control data for apoferritin have been added to this table and are illustrated in Figure 8.	REVIEW_INFO
+75	86	apoferritin	protein_state	We note that we do not reach the experimental maximum loading capacity for apoferritin; however, we also note that the EncFtn-encapsulin nanocompartment sequesters five times more iron than the ferritin under the same reaction conditions, supporting the published observations that these nanocompartments can store more iron than classical ferritin nanocages.	REVIEW_INFO
+137	152	nanocompartment	complex_assembly	We note that we do not reach the experimental maximum loading capacity for apoferritin; however, we also note that the EncFtn-encapsulin nanocompartment sequesters five times more iron than the ferritin under the same reaction conditions, supporting the published observations that these nanocompartments can store more iron than classical ferritin nanocages.	REVIEW_INFO