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.
| Original language | English |
|---|---|
| Article number | 201621 |
| Journal | Scientific data |
| Volume | 3 |
| DOIs | |
| Publication status | Published - Apr 12 2016 |
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ASJC Scopus subject areas
- Education
- Library and Information Sciences
- Computer Science Applications
- Information Systems
- Statistics, Probability and Uncertainty
- Statistics and Probability
Cite this
X-ray laser diffraction for structure determination of the rhodopsin-arrestin complex. / Zhou, X. Edward; Gao, Xiang; Barty, Anton; Kang, Yanyong; He, Yuanzheng; Liu, Wei; Ishchenko, Andrii; White, Thomas A.; Yefanov, Oleksandr; Han, Gye Won; Xu, Qingping; De Waal, Parker W.; Suino-Powell, Kelly M.; Boutet, Sébastien; Williams, Garth J.; Wang, Meitian; Li, Dianfan; Caffrey, Martin; Chapman, Henry N.; Spence, John C H; Fromme, Petra; Weierstall, Uwe; Stevens, Raymond C.; Cherezov, Vadim; Melcher, Karsten; Xu, H. Eric.
In: Scientific data, Vol. 3, 201621, 12.04.2016.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - X-ray laser diffraction for structure determination of the rhodopsin-arrestin complex
AU - Zhou, X. Edward
AU - Gao, Xiang
AU - Barty, Anton
AU - Kang, Yanyong
AU - He, Yuanzheng
AU - Liu, Wei
AU - Ishchenko, Andrii
AU - White, Thomas A.
AU - Yefanov, Oleksandr
AU - Han, Gye Won
AU - Xu, Qingping
AU - De Waal, Parker W.
AU - Suino-Powell, Kelly M.
AU - Boutet, Sébastien
AU - Williams, Garth J.
AU - Wang, Meitian
AU - Li, Dianfan
AU - Caffrey, Martin
AU - Chapman, Henry N.
AU - Spence, John C H
AU - Fromme, Petra
AU - Weierstall, Uwe
AU - Stevens, Raymond C.
AU - Cherezov, Vadim
AU - Melcher, Karsten
AU - Xu, H. Eric
PY - 2016/4/12
Y1 - 2016/4/12
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84963812810&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84963812810&partnerID=8YFLogxK
U2 - 10.1038/sdata.2016.21
DO - 10.1038/sdata.2016.21
M3 - Article
VL - 3
JO - Scientific data
JF - Scientific data
SN - 2052-4463
M1 - 201621
ER -