Enzymology and Dynamics by Cryogenic Electron Microscopy

Cryogenic electron microscopy (cryo-EM) has revolutionized the field of structural biology, particularly in solving the structures of large protein complexes or cellular machineries that play important biological functions. This review focuses on the contribution and future potential of cryo-EM in r...

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Bibliographic Details
Published inAnnual review of biophysics Vol. 51; p. 19
Main Authors Tsai, Ming-Daw, Wu, Wen-Jin, Ho, Meng-Chiao
Format Journal Article
LanguageEnglish
Published United States 09.05.2022
Subjects
Cryoelectron Microscopy - methods
Crystallography, X-Ray
Humans
Ligands
Molecular Conformation
Proteins
dynamics
structural landscape
cryo-EM
enzymology
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Summary:Cryogenic electron microscopy (cryo-EM) has revolutionized the field of structural biology, particularly in solving the structures of large protein complexes or cellular machineries that play important biological functions. This review focuses on the contribution and future potential of cryo-EM in related emerging applications-enzymatic mechanisms and dynamic processes. Work on these subjects can benefit greatly from the capability of cryo-EM to solve the structures of specific protein complexes in multiple conditions, including variations in the buffer condition, ligands, and temperature, and to capture multiple conformational states, conformational change intermediates, and reaction intermediates. These studies can expand the structural landscape of specific proteins or protein complexes in multiple dimensions and drive new advances in the fields of enzymology and dynamic processes. The advantages and complementarity of cryo-EM relative to X-ray crystallography and nuclear magnetic resonance with regard to these applications are also addressed.
ISSN:1936-1238
DOI:10.1146/annurev-biophys-100121-075228