Journal Article PUBDB-2015-02182

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Electronic damage in S atoms in a native protein crystal induced by an intense X-ray free-electron laser pulse

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2015
AIP Publishing LLC Melville, NY

Structural dynamics 2(4), 041703 () [10.1063/1.4919398]
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Abstract: Current hard X-ray free-electron laser (XFEL) sources can deliver doses to biological macromolecules well exceeding 1 GGy, in timescales of a few tens of femtoseconds. During the pulse, photoionization can reach the point of saturation in which certain atomic species in the sample lose most of their electrons. This electronic radiation damage causes the atomic scattering factors to change, affecting, in particular, the heavy atoms, due to their higher photoabsorption cross sections. Here, it is shown that experimental serial femtosecond crystallography data collected with an extremely bright XFEL source exhibit a reduction of the effective scattering power of the sulfur atoms in a native protein. Quantitative methods are developed to retrieve information on the effective ionization of the damaged atomic species from experimental data, and the implications of utilizing new phasing methods which can take advantage of this localized radiation damage are discussed.

Classification:

Note: OA

Contributing Institute(s):
  1. CFEL-Theory (FS-CFEL-3)
Research Program(s):
  1. 6211 - Extreme States of Matter: From Cold Ions to Hot Plasmas (POF3-621) (POF3-621)
  2. 05K13GU7 - Test eines "Serial Femtosecond Crystallography (SFX)"-Messtandes am Europäischen Elektronenlaser XFEL (BMBF-05K13GU7) (BMBF-05K13GU7)
  3. VH-GS-500 - PIER Helmholtz Graduate School (2015_IFV-VH-GS-500) (2015_IFV-VH-GS-500)
Experiment(s):
  1. No specific instrument

Appears in the scientific report 2015
Database coverage:
OpenAccess ; SCOPUS
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 Record created 2015-06-03, last modified 2025-07-17


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