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Electron crystallography of proteins in membranes

Academic Article
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Overview

authors

  • Fujiyoshi, Y.
  • Unwin, Nigel (Peter)

publication date

  • October 2008

journal

  • Current Opinion in Structural Biology  Journal

abstract

  • Electron crystallography has played a vital role in advancing our understanding of proteins in membranes since the 'fluid mosaic model' was proposed in 1972. It is now an established technique to reveal the structures of proteins in their natural bilayer environment and makes possible the study of biological mechanisms through freeze-trapping of transitional states. Thus, images and diffraction patterns of well-ordered, planar and tubular protein-lipid crystals are yielding atomic models, which tell us how the proteins in situ are designed and carry out their membrane-specific tasks. Recent methodological advances and the inclusion of tomographic and cryo-sectioning techniques are enabling detailed information to be obtained from increasingly smaller and more disordered membrane assemblies, extending the potential of this approach.

subject areas

  • Cryoelectron Microscopy
  • Crystallography, X-Ray
  • Electrons
  • Freezing
  • Image Processing, Computer-Assisted
  • Membrane Proteins
  • Models, Molecular
  • Protein Conformation
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Identity

PubMed Central ID

  • PMC2651081

International Standard Serial Number (ISSN)

  • 0959-440X

Digital Object Identifier (DOI)

  • 10.1016/j.sbi.2008.07.005

PubMed ID

  • 18755273
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Additional Document Info

start page

  • 587

end page

  • 592

volume

  • 18

issue

  • 5

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