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Mesoscopic surfactant organization and membrane protein crystallization

  • MICHAEL C. WIENER (a1), ALAN S. VERKMAN (a2), ROBERT M. STROUD (a3) and ALFRED N. VAN HOEK (a4)

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 Å resolution have been obtained with this approach.

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Corresponding author

Reprint requests to: Michael C. Wiener, Department of Molecular Physiology & Biological Physics, University of Virginia, P.O. Box 800736, Charlottesville, Virginia 22908-0736; e-mail: mwiener@virginia.edu.

Keywords

Mesoscopic surfactant organization and membrane protein crystallization

  • MICHAEL C. WIENER (a1), ALAN S. VERKMAN (a2), ROBERT M. STROUD (a3) and ALFRED N. VAN HOEK (a4)

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