Protein structure determination by electron cryo-microscopy.
Transmission electron cryo-microscopy (cryoEM) is a versatile tool in the structural analysis of proteins and biological macromolecular assemblies. In this review, we present a brief survey of the methods used in cryoEM, and their current developments. These latest advances provide exciting opportunities for the three-dimensional structural determination of macromolecular complexes that are either too large or too heterogeneous to be investigated by conventional X-ray crystallography or nuclear magnetic resonance (NMR). The endeavour of understanding the function of protein or macromolecular complex is often helped by combining data from electron microscopy and X-ray crystallography. We will thus provide a brief overview of the computational techniques involved in combining data from different techniques for the interpretation of the EM structure.
Jonic
Slavica
S
IMPMC-UMR 7590, CNRS, Universités Paris 6 et Paris 7, IPGP, 75015 Paris, France.
Vénien-Bryan
Catherine
C
D000818:Animals; D019295:Computational Biology; D003198:Computer Simulation; D020285:Cryoelectron Microscopy; D006801:Humans; D007091:Image Processing, Computer-Assisted; D008958:Models, Molecular; D011487:Protein Conformation; D011506:Proteins / Q000648:ultrastructure*; D013329:Structure-Activity Relationship
D011506:Proteins