X-ray laser diffraction for structure determination of the rhodopsin-arrestin complex

doi:10.1038/sdata.2016.21

KMS > iHuman研究所 > 特聘教授组 > Raymond Stevens组

	X-ray laser diffraction for structure determination of the rhodopsin-arrestin complex
	Zhou, X. Edward 1; Gao, Xiang 1; Barty, Anton 2; Kang, Yanyong 1; He, Yuanzheng 1; Liu, Wei 3,4; Ishchenko, Andrii 5; White, Thomas A.2; Yefanov, Oleksandr 2; Han, Gye Won 5,6; Xu, Qingping 7; de Waal, Parker W.1; Suino-Powell, Kelly M.1; Boutet, Sebastien 8; Williams, Garth J.8; Wang, Meitian 9; Li, Dianfan 10,11; Caffrey, Martin 10,11; Chapman, Henry N.2,12; Spence, John C. H.2,13; Fromme, Petra 2; Weierstall, Uwe 2,13; Stevens, Raymond C.5,6,14 ; Cherezov, Vadim 5; Melcher, Karsten 1; Xu, H. Eric 1,15
	2016-04-12
发表期刊	SCIENTIFIC DATA
ISSN	2052-4463
卷号	3
发表状态	已发表
DOI	10.1038/sdata.2016.21
摘要	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.
收录类别	SCI
语种	英语
资助项目	BMBF project[FKZ 05K12CH1]
WOS研究方向	Science & Technology - Other Topics
WOS类目	Multidisciplinary Sciences
WOS记录号	WOS:000390214400001
出版者	NATURE PUBLISHING GROUP
WOS关键词	SERIAL FEMTOSECOND CRYSTALLOGRAPHY ; LIPIDIC CUBIC PHASE ; INDEXING AMBIGUITY ; CRYSTAL-STRUCTURE ; SPACE-GROUP ; INTEGRATION ; QUALITY
原始文献类型	Article ; Data Paper
引用统计
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/1869
专题	iHuman研究所_特聘教授组_Raymond Stevens组 iHuman研究所
通讯作者	Zhou, X. Edward; Xu, H. Eric
作者单位	1.Van Andel Res Inst, Ctr Struct Biol & Drug Discovery, Lab Struct Sci, Grand Rapids, MI 49503 USA 2.Deutsch Elektronen Synchrotron DESY, Ctr Free Electron Laser Sci, D-22607 Hamburg, Germany 3.Arizona State Univ, Sch Mol Sci, Tempe, AZ 85287 USA 4.Arizona State Univ, Ctr Appl Struct Discovery, Biodesign Inst, Tempe, AZ 85287 USA 5.Univ Southern Calif, Bridge Inst, Dept Chem, Los Angeles, CA 90089 USA 6.Univ Southern Calif, Bridge Inst, Dept Biol Sci, Los Angeles, CA 90089 USA 7.SLAC Natl Accelerator Lab, Stanford Synchrotron Radiat Lightsource, Joint Ctr Struct Genom, Menlo Pk, CA 94025 USA 8.SLAC Natl Accelerator Lab, Linac Coherent Light Source LCLS, Menlo Pk, CA 94025 USA 9.Paul Scherrer Inst, Swiss Light Source, CH-5232 Villigen, Switzerland 10.Trinity Coll Dublin, Sch Med, Dublin D02 R590, Ireland 11.Trinity Coll Dublin, Sch Biochem & Immunol, Dublin D02 R590, Ireland 12.Ctr Ultrafast Imaging, D-22761 Hamburg, Germany 13.Arizona State Univ, Dept Phys, Tempe, AZ 85287 USA 14.Shanghai Tech Univ, IHuman Inst, 2F Bldg 6,99 Haike Rd, Shanghai 201210, Peoples R China 15.Chinese Acad Sci, Shanghai Inst Mat Med, Key Lab Receptor Res, Ctr Struct & Funct Drug Targets,VARI SIMM Ctr, Shanghai 201203, Peoples R China
推荐引用方式 GB/T 7714	Zhou, X. Edward,Gao, Xiang,Barty, Anton,et al. X-ray laser diffraction for structure determination of the rhodopsin-arrestin complex[J]. SCIENTIFIC DATA,2016,3.
APA	Zhou, X. Edward.,Gao, Xiang.,Barty, Anton.,Kang, Yanyong.,He, Yuanzheng.,...&Xu, H. Eric.(2016).X-ray laser diffraction for structure determination of the rhodopsin-arrestin complex.SCIENTIFIC DATA,3.
MLA	Zhou, X. Edward,et al."X-ray laser diffraction for structure determination of the rhodopsin-arrestin complex".SCIENTIFIC DATA 3(2016).