Conformational changes studied by cryo-electron microscopy.

H R Saibil

doi:10.1038/78923

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PubMed · 10966635

Conformational changes studied by cryo-electron microscopy.

H R Saibil

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Abstract

Biological processes involving movement, such as muscle contraction or the opening of an ion channel through a membrane, are mediated through conformational changes. These changes often occur in large and flexible macromolecular complexes. Cryo-electron microscopy provides a means of capturing different conformational states of such assemblies. Even if the resulting density maps are at low resolution, they can be combined with atomic structures of subcomplexes or isolated components determined by X-ray crystallography or NMR. This review presents a brief summary of the principles and recent advances in macromolecular structure determination by cryo-electron microscopy.

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Animals Bacterial Proteins Chaperonins Cryoelectron Microscopy Humans Image Processing, Computer-Assisted Kinetics Models, Molecular Molecular Motor Proteins Protein Conformation Proteins Receptors, Nicotinic Ribosomes Semliki forest virus Streptolysins Journal Article Review

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H R Saibil. 2000. Conformational changes studied by cryo-electron microscopy.. https://doi.org/10.1038/78923

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