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Protein Sci. 2000 Jul;9(7):1407-9.

Mesoscopic surfactant organization and membrane protein crystallization.

Author information

1
Department of Molecular Physiology & Biological Physics, University of Virginia, Charlottesville 22908-0736, USA. mwiener@virginia.edu

Abstract

The paucity of detailed X-ray crystallographic structures of integral membrane proteins arises from substantive technical obstacles in the overexpression of multimilligram quantities of protein, and in the crystallization of purified protein-detergent complexes (PDCs). With rare exception, crystal contacts within the lattice are mediated by protein-protein interaction, and the detergent surrounding the protein behaves as a disordered solvent. The addition and use of surfactants that display mesoscopic self-assembly behavior in membrane protein crystallization experiments presents a novel alternative strategy. Well-ordered crystals of the water channel human aquaporin-1 (hAQP1) that diffract to 4 A resolution have been obtained with this approach.

PMID:
10933509
PMCID:
PMC2144676
DOI:
10.1110/ps.9.7.1407
[Indexed for MEDLINE]
Free PMC Article
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