Mesoscopic surfactant organization and membrane protein crystallization.
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.
Department of Molecular Physiology & Biological Physics, University of Virginia, Charlottesville 22908-0736, USA. mwiener@virginia.edu
M C
MC
Wiener
A S
AS
Verkman
R M
RM
Stroud
A N
AN
van Hoek
D051398:Aquaporin 1; D020346:Aquaporins / Q000737:chemistry*; D001789:Blood Group Antigens; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D003840:Deoxycholic Acid / Q000737:chemistry; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry*; D013501:Surface-Active Agents / Q000737:chemistry*
C496020:AQP1 protein, human; D020346:Aquaporins; D001789:Blood Group Antigens; D008565:Membrane Proteins; D013501:Surface-Active Agents; D003840:Deoxycholic Acid; D051398:Aquaporin 1