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Mesoscopic surfactant organization and membrane protein crystallization

Published online by Cambridge University Press:  01 July 2000

MICHAEL C. WIENER ,
ALAN S. VERKMAN ,
ROBERT M. STROUD  and
ALFRED N. VAN HOEK
MICHAEL C. WIENER
Affiliation:
Department of Molecular Physiology & Biological Physics, University of Virginia, P.O. Box 800736, Charlottesville, Virginia 22908-0736
ALAN S. VERKMAN
Affiliation:
Cardiovascular Research Institute, University of California, 1246 Health Science East Tower, Box 0521, San Francisco, California 94143-0521
ROBERT M. STROUD
Affiliation:
Department of Biochemistry & Biophysics, University of California, S-964, San Francisco, California 94143-0448
ALFRED N. VAN HOEK
Affiliation:
Massachusetts General Hospital, Renal Unit, CNY-8, 32 Fruit St., Boston, Massachusetts 02114
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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.

Keywords

aquaporinbile saltsdetergentsmembrane protein crystallizationself-assembled system
Type
FOR THE RECORD
Information
Protein Science , Volume 9 , Issue 7 , July 2000 , pp. 1407 - 1409
Copyright
2000 The Protein Society

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