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          Institute: MPI für medizinische Forschung     Collection: Jahbruch 2014_archival     Display Documents

ID: 681459.0, MPI für medizinische Forschung / Jahbruch 2014_archival
Anomalous signal from S atoms in protein crystallographic data from an X−ray free−electron laser
Translation of Title:Anomalous signal from S atoms in protein crystallographic data from an X−ray free−electron laser
Authors:Barends, Thomas; Foucar, Lutz; Shoeman, Robert L.; Bari, Sadia; Epp, Sascha W.; Hartmann, Robert; Hauser, Günter; 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, M.; Rolles, Daniel; Rudek, Benedikt; Rudenko, Artem; Sato, Takahiro; Schroeter, Claus Dieter; Soltau, Heike; Strüder, Lothar; Tanaka, Tomoyuki; Togashi, Tadashi; Tono, Kensuke; Ullrich, Joachim; Yase, Satoshi; Wada, Shin−ichi; Yao, Makoto; Yabashi, Makina; Ueda, Kiyoshi; Schlichting, Ilme
Date of Publication (YYYY-MM-DD):2013-05-01
Title of Journal:Acta Crystallographica D
Journal Abbrev.:Acta Crystallogr. Sec. D
Issue / Number:5
Start Page:838
End Page:842
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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
Free Keywords:free−electron lasers; protein crystallography; anomalous diffraction
External Publication Status:published
Document Type:Article
Communicated by:wkaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biophysik
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/Molecular chaperones
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/Analytical Protein Biochemistry
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/Coherent diffractive imaging
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