Journal Article

DESY-2014-01260

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Serial Femtosecond Crystallography of G Protein-Coupled Receptors

Liu, W. (Corresponding author) ; Wacker, D. ; Gati, C.Extern*>CFEL* ; Han, G. W. ; James, D. ; Wang, D. ; Nelson, G. ; Weierstall, U.Extern* ; Katritch, V. ; Barty, A.DESY*>CFEL* ; Zatsepin, N. A. ; Li, D. ; Messerschmidt, M. ; Boutet, S. ; Williams, G. J. ; Koglin, J. E. ; Seibert, M. M. ; Wang, C. ; Shah, S. T. A. ; Basu, S. ; Fromme, R. ; Kupitz, C. ; Rendek, K. N. ; Grotjohann, I. ; Fromme, P. ; Kirian, R.DESY*>CFEL* ; Beyerlein, K.DESY*>CFEL* ; White, T.DESY*>CFEL* ; Chapman, H. N.DESY*>CFEL* ; Caffrey, M. ; Spence, J. C. H. ; Stevens, R. C. ; Cherezov, V.

2013
American Association for the Advancement of Science Washington, DC [u.a.]

This record in other databases:        

Please use a persistent id in citations: doi:10.1126/science.1244142

Abstract: X-ray crystallography of G protein–coupled receptors and other membrane proteins is hampered by difficulties associated with growing sufficiently large crystals that withstand radiation damage and yield high-resolution data at synchrotron sources. We used an x-ray free-electron laser (XFEL) with individual 50-femtosecond-duration x-ray pulses to minimize radiation damage and obtained a high-resolution room-temperature structure of a human serotonin receptor using sub-10-micrometer microcrystals grown in a membrane mimetic matrix known as lipidic cubic phase. Compared with the structure solved by using traditional microcrystallography from cryo-cooled crystals of about two orders of magnitude larger volume, the room-temperature XFEL structure displays a distinct distribution of thermal motions and conformations of residues that likely more accurately represent the receptor structure and dynamics in a cellular environment.

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Contributing Institute(s):

1. CFEL-Coherent X-Ray Imaging (FS-CFEL-1)

Research Program(s):

1. 54x - Programm Forschung mit Photonen, Neutronen, Ionen - Topic unbekannt (POF2-54x) (POF2-54x)

Experiment(s):

1. No specific instrument

Appears in the scientific report 2013

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Database coverage:
; ; BIOSIS Previews ; Current Contents - Agriculture, Biology and Environmental Sciences ; Current Contents - Life Sciences ; Current Contents - Physical, Chemical and Earth Sciences ; JCR ; NCBI Molecular Biology Database ; National-Konsortium ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection ; Zoological Record

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