Cryo-electron microscopy for structural analysis of dynamic biological macromolecules.
BACKGROUND
Since the introduction of what became today's standard for cryo-embedding of biological macromolecules at native conditions more than 30years ago, techniques and equipment have been drastically improved and the structure of biomolecules can now be studied at near atomic resolution by cryo-electron microscopy (cryo-EM) while capturing multiple dynamic states. Here we review the recent progress in cryo-EM for structural studies of dynamic biological macromolecules.


SCOPE OF REVIEW
We provide an overview of the cryo-EM method and introduce contemporary studies to investigate biomolecular structure and dynamics, including examples from the recent literature.


MAJOR CONCLUSIONS
Cryo-EM is a powerful tool for the investigation of biological macromolecular structures including analysis of their dynamics by using advanced image-processing algorithms. The method has become even more widely applicable with present-day single particle analysis and electron tomography.


GENERAL SIGNIFICANCE
The cryo-EM method can be used to determine the three-dimensional structure of biomacromolecules in near native condition at close to atomic resolution, and has the potential to reveal conformations of dynamic molecular complexes. This article is part of a Special Issue entitled "Biophysical Exploration of Dynamical Ordering of Biomolecular Systems" edited by Dr. Koichi Kato.
['Murata|Kazuyoshi|K|', 'Wolf|Matthias|M|']
D000818:Animals D019295:Computational Biology D020285:Cryoelectron Microscopy D006801:Humans D007700:Kinetics D046911:Macromolecular Substances D008954:Models, Biological D056004:Molecular Dynamics Simulation D015394:Molecular Structure D000072760:Single Molecule Imaging D013329:Structure-Activity Relationship
Cryo-electron tomography Electron cryomicroscopy Molecular dynamics Protein structure Single particle 3D reconstruction