Description
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

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.
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    Title
    • Electronic damage in S atoms in a native protein crystal induced by an intense X-ray free-electron laser pulse
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    Date Created
    2015-04-29
    Resource Type
  • Text
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    Identifier
    • Digital object identifier: 10.1063/1.4919398
    • Identifier Type
      International standard serial number
      Identifier Value
      2329-7778
    Note
    • The final version of this article, as published in Structural Dynamics, can be viewed online at: http://aca.scitation.org/doi/10.1063/1.4919398

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    Galli, L., Son, S., Klinge, M., Bajt, S., Barty, A., Bean, R., . . . Chapman, H. N. (2015). Electronic damage in S atoms in a native protein crystal induced by an intense X-ray free-electron laser pulse. Structural Dynamics, 2(4), 041703. doi:10.1063/1.4919398

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