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.