It's not just a phase: crystallization and X-ray structure determination of bacteriorhodopsin in lipidic cubic phases.
Utilization of lipidic cubic phases in the crystallization of bacteriorhodopsin (bR) has yielded long sought after crystals that diffract X-rays to 2 A resolution. The resulting structure provides new information on the protein conformation and the mechanism of proton translocation. Crystallization of bR via lipidic cubic phases may be a harbinger of new membrane protein crystallization strategies.
Gouaux
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Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA. jeg52@columbia.edu
D001426:Bacterial Proteins / Q000737:chemistry; D001436:Bacteriorhodopsins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D019617:Halobacterium salinarum / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry; D008958:Models, Molecular
D001426:Bacterial Proteins; D008565:Membrane Proteins; D001436:Bacteriorhodopsins