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  High-Resolution Electron Crystallography of Membrane Proteins

Kühlbrandt, W. (1994). High-Resolution Electron Crystallography of Membrane Proteins. In S. H. White (Ed.), Methods in Physiology (pp. 206-223 ). New York, NY: American Physiological Society 1994 Springer.

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 Creators:
Kühlbrandt, Werner1, Author                 
Affiliations:
1European Molecular Biology Laboratory, 6900 Heidelberg, Germany, ou_persistent22              

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Free keywords: Purple Membrane; Tilt Axis; Incident Electron Beam; Dimensional Crystal; Electron Crystallography
 Abstract: For the foreseeable future, progress in determining high-resolution structures of membrane proteins will depend on crystallographic techniques. Until recently, x-ray crystallography seemed to be the only promising method. Progress with this technique, however, has not been as rapid as originally hoped because it is difficult to grow large and sufficiently well-ordered three-dimensional crystals. Electron crystallography of two-dimensional crystals is now a viable alternative that is particularly suitable for structural studies of membrane proteins because of their natural propensity to form two-dimensional arrays.

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Language(s): eng - English
 Dates: 1994
 Publication Status: Issued
 Pages: 18
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1007/978-1-4614-7515-6_9
 Degree: -

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Title: Methods in Physiology
  Subtitle : Membrane Protein Structure Experimental Approaches
Source Genre: Series
 Creator(s):
White, Stephen H. 1, Editor
Affiliations:
1 College of Medicine, Department of Physiology and Biophysics, University of California, Irvine, USA, ou_persistent22            
Publ. Info: New York, NY : American Physiological Society 1994 Springer
Pages: 395 Volume / Issue: - Sequence Number: - Start / End Page: 206 - 223 Identifier: DOI: 10.1007/978-1-4614-7515-6
ISBN: 978-1-4614-7515-6