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Medientyp:
E-Artikel
Titel:
Protein structure determination by single-wavelength anomalous diffraction phasing of X-ray free-electron laser data
Beteiligte:
Nass, Karol;
Meinhart, Anton;
Barends, Thomas R. M.;
Foucar, Lutz;
Gorel, Alexander;
Aquila, Andrew;
Botha, Sabine;
Doak, R. Bruce;
Koglin, Jason;
Liang, Mengning;
Shoeman, Robert L.;
Williams, Garth;
Boutet, Sebastien;
Schlichting, Ilme
Erschienen:
International Union of Crystallography (IUCr), 2016
Erschienen in:IUCrJ
Sprache:
Nicht zu entscheiden
DOI:
10.1107/s2052252516002980
ISSN:
2052-2525
Entstehung:
Anmerkungen:
Beschreibung:
<jats:p>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<jats:italic>de novo</jats:italic>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.</jats:p>