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

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 HatsuiPeter 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

研究成果: Article査読

47 被引用数 (Scopus)

抄録

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 Ångstrom 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.

本文言語English
ページ(範囲)838-842
ページ数5
ジャーナルActa Crystallographica Section D: Biological Crystallography
69
5
DOI
出版ステータスPublished - 2013 5

ASJC Scopus subject areas

  • Structural Biology

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