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

Structural Dynamics
Lorenzo GalliHenry N Chapman

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.

References

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Apr 4, 2015·Optics Express·Carl CalemanHenry N Chapman

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Citations

Dec 24, 2016·Journal of Synchrotron Radiation·Elspeth F Garman, Martin Weik
Oct 27, 2018·Structural Dynamics·Nadia L OparaChristian David
Sep 4, 2021·Journal of Synchrotron Radiation·Kajwal Kumar PatraNicusor Timneanu

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Methods Mentioned

BETA
X-ray
RIP

Software Mentioned

Cheetah
Phaser
CrystFEL
CCP
XATOM
REFMAC5

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