Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure

J Mol Biol. 2002 Feb 8;316(1):1-6. doi: 10.1006/jmbi.2001.5295.


Obtaining crystals of membrane proteins that diffract to high resolution remains a major stumbling block in structure determination. Here we present a new method for crystallizing membrane proteins from a bicelle forming lipid/detergent mixture. The method is flexible and simple to use. As a test case, bacteriorhodopsin (bR) from Halobacterium salinarum was crystallized from a bicellar solution, yielding a new bR crystal form. The crystals belong to space group P2(1) with unit cell dimensions of a=45.0 A, b=108.9 A, c=55.9 A, beta=113.58 degrees and a dimeric asymmetric unit. The structure was solved by molecular replacement and refined at 2.0 A resolution. In all previous bR structures the protein is organized as a parallel trimer, but in the crystals grown from bicelles, the individual bR subunits are arranged in an antiparallel fashion.

Publication types

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

MeSH terms

  • Bacteriorhodopsins / chemistry*
  • Bacteriorhodopsins / metabolism*
  • Crystallization
  • Detergents / metabolism*
  • Halobacterium salinarum / chemistry*
  • Lipid Metabolism*
  • Models, Molecular
  • Protein Conformation
  • Solutions
  • X-Ray Diffraction


  • Detergents
  • Solutions
  • Bacteriorhodopsins