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.
| Original language | English |
|---|---|
| Pages (from-to) | 734-736 |
| Number of pages | 3 |
| Journal | Nature Methods |
| Volume | 11 |
| Issue number | 7 |
| DOIs | |
| Publication status | Published - 2014 |
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ASJC Scopus subject areas
- Biotechnology
- Molecular Biology
- Biochemistry
- Cell Biology
Cite this
Determination of damage-free crystal structure of an X-ray-sensitive protein using an XFEL. / Hirata, Kunio; Shinzawa-Itoh, Kyoko; Yano, Naomine; Takemura, Shuhei; Kato, Koji; Hatanaka, Miki; Muramoto, Kazumasa; Kawahara, Takako; Tsukihara, Tomitake; Yamashita, Eiki; Tono, Kensuke; Ueno, Go; Hikima, Takaaki; Murakami, Hironori; Inubushi, Yuichi; Yabashi, Makina; Ishikawa, Tetsuya; Yamamoto, Masaki; Ogura, Takashi; Sugimoto, Hiroshi; Shen, Jian-Ren; Yoshikawa, Shinya; Ago, Hideo.
In: Nature Methods, Vol. 11, No. 7, 2014, p. 734-736.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Determination of damage-free crystal structure of an X-ray-sensitive protein using an XFEL
AU - Hirata, Kunio
AU - Shinzawa-Itoh, Kyoko
AU - Yano, Naomine
AU - Takemura, Shuhei
AU - Kato, Koji
AU - Hatanaka, Miki
AU - Muramoto, Kazumasa
AU - Kawahara, Takako
AU - Tsukihara, Tomitake
AU - Yamashita, Eiki
AU - Tono, Kensuke
AU - Ueno, Go
AU - Hikima, Takaaki
AU - Murakami, Hironori
AU - Inubushi, Yuichi
AU - Yabashi, Makina
AU - Ishikawa, Tetsuya
AU - Yamamoto, Masaki
AU - Ogura, Takashi
AU - Sugimoto, Hiroshi
AU - Shen, Jian-Ren
AU - Yoshikawa, Shinya
AU - Ago, Hideo
PY - 2014
Y1 - 2014
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84903612491&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84903612491&partnerID=8YFLogxK
U2 - 10.1038/nmeth.2962
DO - 10.1038/nmeth.2962
M3 - Article
C2 - 24813624
AN - SCOPUS:84903612491
VL - 11
SP - 734
EP - 736
JO - PLoS Medicine
JF - PLoS Medicine
SN - 1549-1277
IS - 7
ER -