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

作者：Barends Thomas R M^*; Foucar Lutz; Shoeman Robert L; Bari Sadia; Epp Sascha W; Hartmann Robert; Hauser Gunter; Huth Martin; Kieser Christian; Lomb Lukas; Motomura Koji; Nagaya Kiyonobu; Schmidt Carlo; Strecker Rafael; Anielski Denis; Boll Rebecca; Erk Benjamin; Fukuzawa Hironobu; Hartmann Elisabeth; Hatsui Takaki; Holl Peter; Inubushi Yuichi; Ishikawa Tetsuya; Kassemeyer Stephan; Kaiser Christian; Koeck Frank; Kunishima Naoki; Kurka Moritz; Rolles Daniel

来源：Acta Crystallographica Section D-Biological Crystallography, 2013, 69(5): 838-842.

DOI：10.1107/S0907444913002448

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 %26apos;multi-purpose spectroscopy/imaging instrument%26apos; 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.

• 出版日期2013-5
• 单位河北医科大学