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

Barends, T., Foucar, L., Shoeman, R. L., Bari, S., Epp, S. W., Hartmann, R., et al. (2013). Anomalous signal from S atoms in protein crystallographic data from an X-ray free-electron laser. Acta Crystallographica. Section D: Biological Crystallography (Copenhagen), 69(5), 838-842. doi:10.1107/S0907444913002448.

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ActaCrystD_69_2013_838.pdf (beliebiger Volltext), 343KB
 
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 Urheber:
Barends, Thomas1, Autor           
Foucar, Lutz1, Autor           
Shoeman, Robert L.1, Autor           
Bari, Sadia, Autor
Epp, Sascha W., Autor
Hartmann, Robert, Autor
Hauser, Gunter, Autor
Huth, Martin, Autor
Kieser, Christian1, Autor           
Lomb, Lukas1, Autor           
Motomura, Koji, Autor
Nagaya, Kiyonobu, Autor
Schmidt, Carlo, Autor
Strecker, Rafael, Autor
Anielski, Denis, Autor
Boll, Rebecca, Autor
Erk, Benjamin1, Autor           
Fukuzawa, Hironobu, Autor
Hartmann, Elisabeth1, Autor           
Hatsui, Takaki, Autor
Holl, Peter, AutorInubushi, Yuichi, AutorIshikawa, Tetsuya, AutorKassemeyer, Stefan1, Autor           Kaiser, Christian, AutorKoeck, Frank, AutorKunishima, Naoki, AutorKurka, Moritz, AutorRolles, Daniel1, Autor           Rudek, Benedikt1, Autor           Rudenko, Artem, AutorSato, Takahiro, AutorSchroeter, Claus-Dieter, AutorSoltau, Heike, AutorStrueder, Lothar, AutorTanaka, Tomoyuki, AutorTogashi, Tadashi, AutorTono, Kensuke, AutorUllrich, Joachim, AutorYase, Satoshi, AutorWada, Shin-ichi, AutorYao, Makoto, AutorYabashi, Makina, AutorUedag, Kiyoshi, AutorSchlichting, Ilme1, Autor            mehr..
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Schlagwörter: free-electron lasers; protein crystallography; anomalous diffraction
 Zusammenfassung: 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

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Sprache(n): eng - English
 Datum: 2012-10-312013-01-242013-04-112013-05-01
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1107/S0907444913002448
Anderer: 7911
 Art des Abschluß: -

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Titel: Acta Crystallographica. Section D: Biological Crystallography (Copenhagen)
  Kurztitel : Acta Crystallogr D
Genre der Quelle: Zeitschrift
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Seiten: - Band / Heft: 69 (5) Artikelnummer: - Start- / Endseite: 838 - 842 Identifikator: ISSN: 0907-4449
CoNE: https://pure.mpg.de/cone/journals/resource/954925562619