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Structure Analysis of Bacteriorhodopsin by Electron Crystallography

  • J. M. Baldwin
  • T. A. Ceska
  • R. M. Glaeser
  • R. Henderson
Part of the NATO ASI Series book series (NSSA, volume 126)

Abstract

Bacteriorhodopsin (bR) is the protein found in the purple membrane of halobacteria, and it functions as a light-driven proton pump. It comprises a polypeptide chain of 248 amino acids and a light-absorbing chromophore retinal attached to one of the lysine residues. The protein is present in the purple membrane together with lipid molecules and forms a very well ordered two-dimensional array (Oesterhelt and Stoeckenius, 1971; Blaurock and Stoeckenius, 1971).

Keywords

Heavy Atom High Resolution Electron Microscope Native Data Purple Membrane Contrast Transfer Function 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1987

Authors and Affiliations

  • J. M. Baldwin
    • 1
  • T. A. Ceska
    • 1
  • R. M. Glaeser
    • 1
    • 2
  • R. Henderson
    • 1
  1. 1.MRC Laboratory of Molecular BiologyCambridgeEngland
  2. 2.Biophysics DepartmentUniversity of CaliforniaBerkeleyUSA

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