Lipidic cubic phase injector facilitates membrane protein serial femtosecond crystallography

被引：0
|
作者：
Uwe Weierstall
Daniel James
Chong Wang
Thomas A. White
Dingjie Wang
Wei Liu
John C. H. Spence
R. Bruce Doak
Garrett Nelson
Petra Fromme
Raimund Fromme
Ingo Grotjohann
Christopher Kupitz
Nadia A. Zatsepin
Haiguang Liu
Shibom Basu
Daniel Wacker
Gye Won Han
Vsevolod Katritch
Sébastien Boutet
Marc Messerschmidt
Garth J. Williams
Jason E. Koglin
M. Marvin Seibert
Markus Klinker
Cornelius Gati
Robert L. Shoeman
Anton Barty
Henry N. Chapman
Richard A. Kirian
Kenneth R. Beyerlein
Raymond C. Stevens
Dianfan Li
Syed T. A. Shah
Nicole Howe
Martin Caffrey
Vadim Cherezov
机构：
[1] Arizona State University,Department of Physics
[2] The Scripps Research Institute,Department of Integrative Structural and Computational Biology
[3] Center for Free-Electron Laser Science,Department of Chemistry and Biochemistry
[4] DESY,Department of Cell and Molecular Biology
[5] Notkestrasse 85,Departamento de Química
[6] Arizona State University,Department of Physics
[7] SLAC National Accelerator Laboratory,undefined
[8] 2575 Sand Hill Road,undefined
[9] Laboratory of Molecular Biophysics,undefined
[10] Uppsala University,undefined
[11] Husargatan 3 (Box 596),undefined
[12] Universidad Autónoma de Madrid,undefined
[13] Ciudad Universitaria de Cantoblanco,undefined
[14] Max-Planck-Institut für medizinische Forschung,undefined
[15] Jahnstrasse 29,undefined
[16] University of Hamburg,undefined
[17] Center for Ultrafast Imaging,undefined
[18] School of Medicine and School of Biochemistry and Immunology,undefined
[19] Trinity College,undefined
来源：
Nature Communications | / 5卷
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摘要：
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.
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