Journal Article

PUBDB-2016-04951

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png X-ray laser diffraction for structure determination of the rhodopsin-arrestin complex

Zhou, X. E. (Corresponding author) ; Gao, X. ; Barty, A.CFEL*DESY* ; Kang, Y. ; He, Y. ; liu, w.Extern* ; Ishchenko, A. ; White, T.CFEL*DESY* ; Yefanov, O.CFEL*EMBL*DESY* ; Han, G. W. ; Xu, Q. ; de Waal, P. W. ; Suino-Powell, K. M. ; Boutet, S.Extern* ; Williams, G. J. ; Wang, M. ; Li, D. ; Caffrey, M. ; Chapman, H. N.CFEL*DESY* ; Spence, J. C. H. ; Fromme, P.Extern* ; Weierstall, U.Extern* ; Stevens, R. C. ; Cherezov, V. ; Melcher, K. ; Xu, H. E. (Corresponding author)

2016
Nature Publ. Group London

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Please use a persistent id in citations: doi:10.1038/sdata.2016.21  doi:10.3204/PUBDB-2016-04951

Abstract: Serial femtosecond X-ray crystallography (SFX) using an X-ray free electron laser (XFEL) is a recent advancement in structural biology for solving crystal structures of challenging membrane proteins, including G-protein coupled receptors (GPCRs), which often only produce microcrystals. An XFEL delivers highly intense X-ray pulses of femtosecond duration short enough to enable the collection of single diffraction images before significant radiation damage to crystals sets in. Here we report the deposition of the XFEL data and provide further details on crystallization, XFEL data collection and analysis, structure determination, and the validation of the structural model. The rhodopsin-arrestin crystal structure solved with SFX represents the first near-atomic resolution structure of a GPCR-arrestin complex, provides structural insights into understanding of arrestin-mediated GPCR signaling, and demonstrates the great potential of this SFX-XFEL technology for accelerating crystal structure determination of challenging proteins and protein complexes.

Note: URL of special issue: http://www.nature.com/sdata/collections/xfel-biodata

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Contributing Institute(s):

1. CFEL-Coherent X-Ray Imaging (FS-CFEL-1)
2. FS-CFEL-1 (Group Leader: Henry Chapman) (CFEL-I)

Research Program(s):

1. 6215 - Soft Matter, Health and Life Sciences (POF3-621) (POF3-621)
2. CUI - Hamburger Zentrum für ultraschnelle Beobachtung (194651731) (194651731)

Experiment(s):

1. Measurement at external facility

Appears in the scientific report 2016

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Database coverage:
; ; ; ; DOAJ Seal ; NCBI Molecular Biology Database

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