FEBS Lett. 1999 Aug 27;457(2):205-8.

Detergent-free membrane protein crystallization.

Nollert P, Royant A, Pebay-Peyroula E, Landau EM.

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Department of Molecular Microbiology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056, Basel, Switzerland.

Abstract

A comprehensive understanding of structure-function relationships of proteins requires their structures to be elucidated to high resolution. With most membrane proteins this has not been accomplished so far, mainly because of their notoriously poor crystallizability. Here we present a completely detergent-free procedure for the incorporation of a native purple membrane into a monoolein-based lipidic cubic phase, and subsequent crystallization of three-dimensional bacteriorhodopsin crystals therein. These crystals exhibit comparable X-ray diffraction quality and mosaicity, and identical crystal habit and space group to those of bacteriorhodopsin crystals that are grown from detergent-solubilized protein in cubic phase.

PMID:: 10471779; [PubMed - indexed for MEDLINE]

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A novel three-dimensional crystal of bacteriorhodopsin obtained by successive fusion of the vesicular assemblies. [J Mol Biol. 1998]
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Cited by 3 PubMed Central articles

Effects of impurities on membrane-protein crystallization in different systems. [Acta Crystallogr D Biol Crysta...]
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Kors CA, Wallace E, Davies DR, Li L, Laible PD, Nollert P. Acta Crystallogr D Biol Crystallogr. 2009 Oct; 65(Pt 10):1062-73. Epub 2009 Sep 16.
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Lipidic cubic phases as matrices for membrane protein crystallization.
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Self diffusion and spectral modifications of a membrane protein, the Rubrivivax gelatinosus LH2 complex, incorporated into a monoolein cubic phase.
Tsapis N, Reiss-Husson F, Ober R, Genest M, Hodges RS, Urbach W. Biophys J. 2001 Sep; 81(3):1613-23.

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