| Literature DB >> 24813624 |
Kunio Hirata1, Kyoko Shinzawa-Itoh2, Naomine Yano3, Shuhei Takemura4, Koji Kato2, Miki Hatanaka4, Kazumasa Muramoto4, Takako Kawahara4, Tomitake Tsukihara5, Eiki Yamashita6, Kensuke Tono7, Go Ueno8, Takaaki Hikima8, Hironori Murakami8, Yuichi Inubushi8, Makina Yabashi8, Tetsuya Ishikawa8, Masaki Yamamoto8, Takashi Ogura9, Hiroshi Sugimoto8, Jian-Ren Shen10, Shinya Yoshikawa4, Hideo Ago8.
Abstract
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.Entities:
Mesh:
Substances:
Year: 2014 PMID: 24813624 DOI: 10.1038/nmeth.2962
Source DB: PubMed Journal: Nat Methods ISSN: 1548-7091 Impact factor: 28.547