Protein structure determination by electron cryo-microscopy

Curr Opin Pharmacol. 2009 Oct;9(5):636-42. doi: 10.1016/j.coph.2009.04.006. Epub 2009 May 22.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Computational Biology
  • Computer Simulation
  • Cryoelectron Microscopy*
  • Humans
  • Image Processing, Computer-Assisted
  • Models, Molecular
  • Protein Conformation
  • Proteins / ultrastructure*
  • Structure-Activity Relationship

Substances

  • Proteins