Journal Article PUBDB-2015-04279

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Towards phasing using high X-ray intensity

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2015
International Union of Crystallography (IUCr) Chester

IUCrJ 2(6), 1-8 () [10.1107/S2052252515014049]
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Abstract: X-ray free-electron lasers (XFELs) show great promise for macromolecular structure determination from sub-micrometre-sized crystals, using the emerging method of serial femtosecond crystallography. The extreme brightness of the XFEL radiation can multiply ionize most, if not all, atoms in a protein, causing their scattering factors to change during the pulse, with a preferential ‘bleaching’ of heavy atoms. This paper investigates the effects of electronic damage on experimental data collected from a Gd derivative of lysozyme microcrystals at different X-ray intensities, and the degree of ionization of Gd atoms is quantified from phased difference Fourier maps. A pattern sorting scheme isproposed to maximize the ionization contrast and the way in which the local electronic damage can be used for a new experimental phasing method is discussed.

Classification:

Contributing Institute(s):
  1. CFEL-Coherent X-Ray Imaging (FS-CFEL-1)
  2. CFEL-Theory (FS-CFEL-3)
Research Program(s):
  1. 6215 - Soft Matter, Health and Life Sciences (POF3-621) (POF3-621)
  2. 05E13GU1 - Entwicklung eines "Serial Femtosecond Crystallography (SFX)"-Messtandes am Europäischen Elektronenlaser XFEL (BMBF-05E13GU1) (BMBF-05E13GU1)
Experiment(s):
  1. Experiments at CFEL

Appears in the scientific report 2015
Database coverage:
Medline ; Creative Commons Attribution CC BY 2.0 ; DOAJ ; OpenAccess ; Current Contents - Physical, Chemical and Earth Sciences ; NCBI Molecular Biology Database ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection
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Private Collections > >DESY > >FS > FS-CFEL-3
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 Record created 2015-10-21, last modified 2025-07-17


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