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Structure of Bacteriorhdopsin Transferred from Amphipol A8-35 to a Lipidic MesophaseStructure of Bacteriorhdopsin Transferred from Amphipol A8-35 to a Lipidic Mesophase
Structural highlights
FunctionBACR_HALSA Light-driven proton pump. Publication Abstract from PubMedAmphipols (APols) have become important tools for the stabilization, folding, and in vitro structural and functional studies of membrane proteins (MPs). Direct crystallization of MPs solubilized in APols would be of high importance for structural biology. However, despite considerable efforts, it is still not clear whether MP/APol complexes can form well-ordered crystals suitable for X-ray crystallography. In the present work, we show that an APol-trapped MP can be crystallized in meso. Bacteriorhodopsin (BR) trapped by APol A8-35 was mixed with a lipidic mesophase, and crystallization was induced by adding a precipitant. The crystals diffract beyond 2 A. The structure of BR was solved to 2 A and found to be indistinguishable from previous structures obtained after transfer from detergent solutions. We suggest the proposed protocol of in meso crystallization to be generally applicable to APol-trapped MPs. High-Resolution Structure of a Membrane Protein Transferred from Amphipol to a Lipidic Mesophase.,Polovinkin V, Gushchin I, Sintsov M, Round E, Balandin T, Chervakov P, Schevchenko V, Utrobin P, Popov A, Borshchevskiy V, Mishin A, Kuklin A, Willbold D, Chupin V, Popot JL, Gordeliy V J Membr Biol. 2014 Sep 6. PMID:25192977[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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