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Large complexes and molecular machines by electron microscopy

Part 3. Proteomics

3.7. Structural Proteomics

Short Specialist Review

  1. J. M. Plitzko,
  2. H. Engelhardt

Published Online: 15 APR 2005

DOI: 10.1002/047001153X.g307311

Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics

Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics

How to Cite

Plitzko, J. M. and Engelhardt, H. 2005. Large complexes and molecular machines by electron microscopy. Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics. 3:3.7:100.

Author Information

  1. Max-Planck-Institute of Biochemistry, Martinsried, Germany

Publication History

  1. Published Online: 15 APR 2005

Abstract

Cryo-electron tomography has the unique potential of visualizing the structure of large protein complexes in isolated preparations at high resolution and in their natural context, in unperturbed cells. Tomograms of vitrified cells are essentially three-dimensional images of their entire proteome. They contain the information of the spatial relationship of macromolecules, their interactions, and reveal the assembly of macromolecular machines that are only stable in vivo. Here, we present a brief survey of the principles and developments of cryo-electron microscopy and image reconstruction.

Keywords:

  • transmission electron microscopy (TEM);
  • cryo-preparation;
  • cryo-EM;
  • electron tomography