論文

査読有り
2013年5月

Anomalous signal from S atoms in protein crystallographic data from an X-ray free-electron laser

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
  • Thomas R. M. Barends
  • Lutz Foucar
  • Robert L. Shoeman
  • Sadia Bari
  • Sascha W. Epp
  • Robert Hartmann
  • Gunter Hauser
  • Martin Huth
  • Christian Kieser
  • Lukas Lomb
  • Koji Motomura
  • Kiyonobu Nagaya
  • Carlo Schmidt
  • Rafael Strecker
  • Denis Anielski
  • Rebecca Boll
  • Benjamin Erk
  • Hironobu Fukuzawa
  • Elisabeth Hartmann
  • Takaki Hatsui
  • Peter Holl
  • Yuichi Inubushi
  • Tetsuya Ishikawa
  • Stephan Kassemeyer
  • Christian Kaiser
  • Frank Koeck
  • Naoki Kunishima
  • Moritz Kurka
  • Daniel Rolles
  • Benedikt Rudek
  • Artem Rudenko
  • Takahiro Sato
  • Claus-Dieter Schroeter
  • Heike Soltau
  • Lothar Strueder
  • Tomoyuki Tanaka
  • Tadashi Togashi
  • Kensuke Tono
  • Joachim Ullrich
  • Satoshi Yase
  • Shin-ichi Wada
  • Makoto Yao
  • Makina Yabashi
  • Kiyoshi Ueda
  • Ilme Schlichting
  • 全て表示

69
5
開始ページ
838
終了ページ
842
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1107/S0907444913002448
出版者・発行元
WILEY-BLACKWELL

X-ray free-electron lasers (FELs) enable crystallographic data collection using extremely bright femtosecond pulses from microscopic crystals beyond the limitations of conventional radiation damage. This diffraction-before-destruction approach requires a new crystal for each FEL shot and, since the crystals cannot be rotated during the X-ray pulse, data collection requires averaging over many different crystals and a Monte Carlo integration of the diffraction intensities, making the accurate determination of structure factors challenging. To investigate whether sufficient accuracy can be attained for the measurement of anomalous signal, a large data set was collected from lysozyme microcrystals at the newly established 'multi-purpose spectroscopy/imaging instrument' of the SPring-8 Angstrom Compact Free-Electron Laser (SACLA) at RIKEN Harima. Anomalous difference density maps calculated from these data demonstrate that serial femtosecond crystallography using a free-electron laser is sufficiently accurate to measure even the very weak anomalous signal of naturally occurring S atoms in a protein at a photon energy of 7.3 keV.

リンク情報
DOI
https://doi.org/10.1107/S0907444913002448
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000318240200018&DestApp=WOS_CPL
ID情報
  • DOI : 10.1107/S0907444913002448
  • ISSN : 0907-4449
  • Web of Science ID : WOS:000318240200018

エクスポート
BibTeX RIS