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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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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-8FDE-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-8FDF-6
Genre: Journal Article

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 Creators:
Barends, Thomas1, Author              
Foucar, Lutz1, Author              
Shoeman, Robert L.1, Author              
Bari, Sadia, Author
Epp, Sascha W., Author
Hartmann, Robert, Author
Hauser, Gunter, Author
Huth, Martin, Author
Kieser, Christian1, Author              
Lomb, Lukas1, Author              
Motomura, Koji, Author
Nagaya, Kiyonobu, Author
Schmidt, Carlo, Author
Strecker, Rafael, Author
Anielski, Denis, Author
Boll, Rebecca, Author
Erk, Benjamin1, Author              
Fukuzawa, Hironobu, Author
Hartmann, Elisabeth1, Author              
Hatsui, Takaki, Author
Holl, Peter, AuthorInubushi, Yuichi, AuthorIshikawa, Tetsuya, AuthorKassemeyer, Stefan1, Author              Kaiser, Christian, AuthorKoeck, Frank, AuthorKunishima, Naoki, AuthorKurka, Moritz, AuthorRolles, Daniel1, Author              Rudek, Benedikt1, Author              Rudenko, Artem, AuthorSato, Takahiro, AuthorSchroeter, Claus-Dieter, AuthorSoltau, Heike, AuthorStrueder, Lothar, AuthorTanaka, Tomoyuki, AuthorTogashi, Tadashi, AuthorTono, Kensuke, AuthorUllrich, Joachim, AuthorYase, Satoshi, AuthorWada, Shin-ichi, AuthorYao, Makoto, AuthorYabashi, Makina, AuthorUedag, Kiyoshi, AuthorSchlichting, Ilme1, Author               more..
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: free-electron lasers; protein crystallography; anomalous diffraction
 Abstract: 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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Language(s): eng - English
 Dates: 2012-10-312013-01-242013-04-112013-05-01
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1107/S0907444913002448
Other: 7911
 Degree: -

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Title: Acta Crystallographica. Section D: Biological Crystallography (Copenhagen)
  Abbreviation : Acta Crystallogr D
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 69 (5) Sequence Number: - Start / End Page: 838 - 842 Identifier: ISSN: 0907-4449
CoNE: https://pure.mpg.de/cone/journals/resource/954925562619