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

X. Edward Zhou, Xiang Gao, Anton Barty, Yanyong Kang, Yuanzheng He, Wei Liu, Andrii Ishchenko, Thomas A. White, Oleksandr Yefanov, Gye Won Han, Qingping Xu, Parker W. De Waal, Kelly M. Suino-Powell, Sébastien Boutet, Garth J. Williams, Meitian Wang, Dianfan Li, Martin Caffrey, Henry N. Chapman, John C H Spence & 6 others Petra Fromme, Uwe Weierstall, Raymond C. Stevens, Vadim Cherezov, Karsten Melcher, H. Eric Xu

Research output: Contribution to journalArticle

19 Citations (Scopus)

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 languageEnglish
Article number201621
JournalScientific data
Volume3
DOIs
Publication statusPublished - Apr 12 2016

Fingerprint

X ray lasers
X-ray Laser
Free Electron Laser
Free electron lasers
Femtosecond
Diffraction
G Protein
Proteins
Crystal Structure
X ray crystallography
Receptor
Crystal structure
Protein
Radiation Damage
Membrane Protein
Structural Model
Crystallization
Microcrystals
structural model
Radiation damage

ASJC Scopus subject areas

  • Education
  • Library and Information Sciences
  • Computer Science Applications
  • Information Systems
  • Statistics, Probability and Uncertainty
  • Statistics and Probability

Cite this

Zhou, X. E., Gao, X., Barty, A., Kang, Y., He, Y., Liu, W., ... Xu, H. E. (2016). X-ray laser diffraction for structure determination of the rhodopsin-arrestin complex. Scientific data, 3, [201621]. https://doi.org/10.1038/sdata.2016.21

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 journalArticle

Zhou, XE, Gao, X, Barty, A, Kang, Y, He, Y, Liu, W, Ishchenko, A, White, TA, Yefanov, O, Han, GW, Xu, Q, De Waal, PW, Suino-Powell, KM, Boutet, S, Williams, GJ, Wang, M, Li, D, Caffrey, M, Chapman, HN, Spence, JCH, Fromme, P, Weierstall, U, Stevens, RC, Cherezov, V, Melcher, K & Xu, HE 2016, 'X-ray laser diffraction for structure determination of the rhodopsin-arrestin complex', Scientific data, vol. 3, 201621. https://doi.org/10.1038/sdata.2016.21
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. / X-ray laser diffraction for structure determination of the rhodopsin-arrestin complex. In: Scientific data. 2016 ; Vol. 3.
@article{b0b404270e0645acb47efe34c308db76,
title = "X-ray laser diffraction for structure determination of the rhodopsin-arrestin complex",
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.",
author = "Zhou, {X. Edward} and Xiang Gao and Anton Barty and Yanyong Kang and Yuanzheng He and Wei Liu and Andrii Ishchenko and White, {Thomas A.} and Oleksandr Yefanov and Han, {Gye Won} and Qingping Xu and {De Waal}, {Parker W.} and Suino-Powell, {Kelly M.} and S{\'e}bastien Boutet and Williams, {Garth J.} and Meitian Wang and Dianfan Li and Martin Caffrey and Chapman, {Henry N.} and Spence, {John C H} and Petra Fromme and Uwe Weierstall and Stevens, {Raymond C.} and Vadim Cherezov and Karsten Melcher and Xu, {H. Eric}",
year = "2016",
month = "4",
day = "12",
doi = "10.1038/sdata.2016.21",
language = "English",
volume = "3",
journal = "Scientific data",
issn = "2052-4463",
publisher = "Nature Publishing Group",

}

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 -