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

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...

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Bibliographic Details
Published in:	Acta crystallographica. Section D, Biological crystallography. Vol. 69; no. 5; pp. 838 - 842
Main 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
Format:	Journal Article
Language:	English
Published:	5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01-05-2013 Wiley Subscription Services, Inc
Subjects:	anomalous diffraction Crystal structure Crystallography Crystallography, X-Ray - instrumentation Crystallography, X-Ray - methods Cysteine - chemistry Data acquisition Density Diffraction Free electron lasers Lasers Models, Molecular Muramidase - chemistry Protein Conformation protein crystallography Proteins Sulfur - chemistry X-rays anomalous diffraction protein crystallography free-electron lasers
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Summary:	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.
Bibliography:	ArticleID:AYDCB5024 istex:E082973827CA8E53A2E5FC196FAEC1FCBFF8B58D ark:/67375/WNG-LP005BW2-B ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-1
ISSN:	1399-0047 0907-4449 1399-0047
DOI:	10.1107/S0907444913002448