Two-dimensional crystallization of proteins on planar lipid films and structure determination by electron crystallography

Alain Brisson, Anders Olofsson, Philippe Ringler, Marc Schmutz, Svetla Stoylova

Research output: Contribution to journalArticle

49 Scopus citations

Abstract

Electron crystallography constitutes a powerful new method for determining the struture of biological macromolecules. This method is best adapted to the study of ordered assemblies of macromolecules, and principally to two-dimensional (2-D) crystals of proteins. Obtaining protein 2-D crystals ordered at high resolution constitutes the major limiting step in the application of this approach. Considerable interest has been raised by the development of a rational method of 2-D crystallization based on the specific binding of proteins to planar lipid films. The applicability of this method is quasi-general in the case of soluble proteins. Its basic principles, together with examples taken from work in our group, are presented here.

Original languageEnglish (US)
Pages (from-to)221-228
Number of pages8
JournalBiology of the Cell
Volume80
Issue number2-3
StatePublished - 1994

Keywords

  • 2-D crystals
  • electron crystallography
  • membrane-bound proteins
  • planar lipid films

ASJC Scopus subject areas

  • Cell Biology

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    Brisson, A., Olofsson, A., Ringler, P., Schmutz, M., & Stoylova, S. (1994). Two-dimensional crystallization of proteins on planar lipid films and structure determination by electron crystallography. Biology of the Cell, 80(2-3), 221-228.