X-ray Laser Diffraction for Structure Determination of the Rhodopsin-arrestin Complex

Overview

Journal Sci Data

Specialty Science

Date 2016 Apr 13

PMID 27070998

Citations 24

Authors

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

Sebastien Boutet

Garth J Williams

Meitian Wang

Dianfan Li

Martin Caffrey

Henry N Chapman

John C H Spence

Petra Fromme

Uwe Weierstall

Raymond C Stevens

Vadim Cherezov

Karsten Melcher

H Eric Xu

Affiliations

Soon will be listed here.

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.

Citing Articles

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