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Two‐dimensional crystallization of proteins on planar lipid films and structure determination by electron crystallography *
Author(s) -
Brisson Alain,
Olofsson Anders,
Ringler Philippe,
Schmutz Marc,
Stoylova Svetla
Publication year - 1994
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1111/j.1768-322x.1994.tb00933.x
Subject(s) - macromolecule , crystallization , protein crystallization , limiting , resolution (logic) , crystallography , planar , electron crystallography , high resolution , electron , materials science , electron diffraction , biology , diffraction , chemistry , physics , biochemistry , computer science , optics , organic chemistry , mechanical engineering , computer graphics (images) , remote sensing , artificial intelligence , geology , engineering , quantum mechanics
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.