Anomalous signal from S atoms in protein crystallographic data from an X‐ray free‐electron laser. (1st May 2013)

• Record Type: Journal Article
• Authors: 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; Rudek, Benedikt; Rudenko, Artem; Sato, Takahiro; Schroeter, Claus‐Dieter; Soltau, Heike; Strueder, Lothar; Tanaka, Tomoyuki; Togashi, Tadashi; Tono, Kensuke; Ullrich, Joachim; Yase, Satoshi; Wada, Shin‐ichi; Yao, Makoto; Yabashi, Makina; Ueda, Kiyoshi; Schlichting, Ilme;
• Is Part Of: Acta crystallographica. Volume 69:Part 5(2013:May)
• Page Start: 838
• Page End: 842
• Publication Date: 2013-05-01
• Subjects: Biomolecules -- Structure -- Periodicals; Physical biochemistry -- Periodicals; X-ray crystallography -- Periodicals; Crystallography -- Periodicals; 572
• DOI: 10.1107/S0907444913002448
• Languages: English
• ISSNs: 0907-4449

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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.</p> </abstract>