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Electronic damage in S atoms in a native protein crystal induced by an intense X-ray free-electron laser pulse
Deutsch Elektronen Synchrotron DESY, Ctr Free Electron Laser Sci, D-22607 Hamburg, Germany.;Univ Hamburg, Dept Phys, D-20355 Hamburg, Germany..
Univ Hamburg, Inst Biochem & Mol Biol, Joint Lab Struct Biol Infect & Inflammat, D-22607 Hamburg, Germany.;Univ Lubeck, Inst Biochem, DESY, D-22607 Hamburg, Germany..
Deutsch Elektronen Synchrotron DESY, Photon Sci, D-22607 Hamburg, Germany..
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2015 (English)In: STRUCTURAL DYNAMICS, ISSN 2329-7778, Vol. 2, no 4, 041703Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2015. Vol. 2, no 4, 041703
National Category
Chemical Sciences Physical Sciences
URN: urn:nbn:se:uu:diva-263539DOI: 10.1063/1.4919398ISI: 000360649200005OAI: diva2:858843
Swedish Research CouncilSwedish Foundation for Strategic Research
Available from: 2015-10-05 Created: 2015-10-02 Last updated: 2015-10-05Bibliographically approved

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