| Literature DB >> 24525480 |
Uwe Weierstall1, Daniel James1, Chong Wang2, Thomas A White3, Dingjie Wang1, Wei Liu2, John C H Spence1, R Bruce Doak1, Garrett Nelson1, Petra Fromme4, Raimund Fromme4, Ingo Grotjohann4, Christopher Kupitz4, Nadia A Zatsepin1, Haiguang Liu1, Shibom Basu4, Daniel Wacker2, Gye Won Han2, Vsevolod Katritch2, Sébastien Boutet5, Marc Messerschmidt5, Garth J Williams5, Jason E Koglin5, M Marvin Seibert6, Markus Klinker7, Cornelius Gati3, Robert L Shoeman8, Anton Barty3, Henry N Chapman9, Richard A Kirian10, Kenneth R Beyerlein3, Raymond C Stevens2, Dianfan Li11, Syed T A Shah11, Nicole Howe11, Martin Caffrey11, Vadim Cherezov2.
Abstract
Lipidic cubic phase (LCP) crystallization has proven successful for high-resolution structure determination of challenging membrane proteins. Here we present a technique for extruding gel-like LCP with embedded membrane protein microcrystals, providing a continuously renewed source of material for serial femtosecond crystallography. Data collected from sub-10-μm-sized crystals produced with less than 0.5 mg of purified protein yield structural insights regarding cyclopamine binding to the Smoothened receptor.Entities:
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Year: 2014 PMID： 24525480 PMCID： PMC4061911 DOI： 10.1038/ncomms4309
Source DB: PubMed Journal: Nat Commun ISSN： 2041-1723 Impact factor: 14.919