Determination of damage-free crystal structure of an X-ray-sensitive protein using an XFEL

被引：0

作者：

Hirata K. ^{[1
,2
]}

Shinzawa-Itoh K. ^{[3
]}

Yano N. ^{[2
,3
]}

Takemura S. ^{[3
]}

Kato K. ^{[3
,8
]}

Hatanaka M. ^{[3
]}

Muramoto K. ^{[3
]}

Kawahara T. ^{[3
]}

Tsukihara T. ^{[2
,3
,4
]}

Yamashita E. ^{[4
]}

Tono K. ^{[5
]}

Ueno G. ^{[1
]}

Hikima T. ^{[1
]}

Murakami H. ^{[1
]}

Inubushi Y. ^{[1
]}

Yabashi M. ^{[1
]}

Ishikawa T. ^{[1
]}

Yamamoto M. ^{[1
]}

Ogura T. ^{[6
]}

Sugimoto H. ^{[1
]}

Shen J.-R. ^{[7
]}

Yoshikawa S. ^{[3
]}

Ago H. ^{[1
]}

机构：

[1] RIKEN SPring-8 Center, Sayo

[2] Japan Science and Technology Agency (JST), Core Research for Evolutional Science and Technology (CREST), Kawaguchi

[3] Picobiology Institute, Graduate School of Life Science, University of Hyogo, Kamigori-cho

[4] Institute for Protein Research, Osaka University, Suita

[5] Japan Synchrotron Radiation Research Institute, Sayo

[6] Picobiology Institute, Graduate School of Life Science, University of Hyogo, Sayo

[7] Photosynthesis Research Center, Graduate School of Natural Science and Technology, Okayama University, Okayama

[8] Faculty of Advanced Life Science, Hokkaido University, Sapporo

来源：

Nature Methods | 2014年 / 11卷 / 7期

基金：

日本学术振兴会;

关键词：

D O I：

10.1038/nmeth.2962

中图分类号：

学科分类号：

摘要：

We report a method of femtosecond crystallography for solving radiation damage-free crystal structures of large proteins at sub-angstrom spatial resolution, using a large single crystal and the femtosecond pulses of an X-ray free-electron laser (XFEL). We demonstrated the performance of the method by determining a 1.9-Å radiation damage-free structure of bovine cytochrome c oxidase, a large (420-kDa), highly radiation-sensitive membrane protein.

引用

页码：734 / 736

页数：2

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