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  Protein structure determination by single-wavelength anomalous diffraction phasing of X-ray free-electron laser data

Nass, K., Meinhart, A., Barends, T. R. M., Foucar, L., Gorel, A., Aquila, A., et al. (2016). Protein structure determination by single-wavelength anomalous diffraction phasing of X-ray free-electron laser data. IUCrJ, 3(3), 180-191. doi:10.1107/S2052252516002980.

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IUCrJ_epub_2016_980.pdf (beliebiger Volltext), 2MB
 
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 Urheber:
Nass, Karol1, Autor           
Meinhart, Anton1, Autor           
Barends, Thomas R. M.1, Autor           
Foucar, Lutz1, Autor           
Gorel, Alexander1, Autor           
Aquila, Andrew, Autor
Botha, Sabine1, Autor           
Doak, R. Bruce1, Autor           
Koglin, Jason, Autor
Liang, Mengning, Autor
Shoeman, Robert L.1, Autor           
Williams, Garth, Autor
Boutet, Sebastien, Autor
Schlichting, Ilme1, Autor           
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Schlagwörter: serial femtosecond crystallography; SFX; X-ray free-electron lasers; XFELs; SAD phasing; single-wavelength anomalous diffraction
 Zusammenfassung: Serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs) offers unprecedented possibilities for macromolecular structure determination of systems that are prone to radiation damage. However, phasing XFEL data de novo is complicated by the inherent inaccuracy of SFX data, and only a few successful examples, mostly based on exceedingly strong anomalous or isomorphous difference signals, have been reported. Here, it is shown that SFX data from thaumatin microcrystals can be successfully phased using only the weak anomalous scattering from the endogenous S atoms. Moreover, a step-by-step investigation is presented of the particular problems of SAD phasing of SFX data, analysing data from a derivative with a strong anomalous signal as well as the weak signal from endogenous S atoms.

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Sprache(n): eng - English
 Datum: 2015-12-242016-02-182016-05-012016-05-09
 Publikationsstatus: Erschienen
 Seiten: 12
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
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Titel: IUCrJ
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Chester : International Union of Crystallography
Seiten: - Band / Heft: 3 (3) Artikelnummer: - Start- / Endseite: 180 - 191 Identifikator: ISSN: 2052-2525