Structural dynamics in proteins induced by and probed with X-ray free-electron 
laser pulses

Nass, Karol; Gorel, Alexander; Abdullah, Malik M.; Martin, Andrew V.; Kloos, Marco; Marinelli, Agostino; Aquila, Andrew; Barends, Thomas R. M.; Decker, Franz-Josef; Doak, R. Bruce; Foucar, Lutz; Hartmann, Elisabeth; Hilpert, Mario; Hunter, Mark S.; Jurek, Zoltan; Koglin, Jason E.; Kozlov, Alexander; Lutman, Alberto A.; Nass Kovács, Gabriela; Roome, Christopher M.; Shoeman, Robert L.; Santra, Robin; Quiney, Harry M.; Ziaja, Beata; Boutet, Sébastien; Schlichting, Ilme

doi:10.1038/s41467-020-15610-4

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Structural dynamics in proteins induced by and probed with X-ray free-electron laser pulses

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Nass, Karol
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons192083

Gorel, Alexander
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons203860

Kloos, Marco
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons92083

Barends, Thomas R. M.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons117878

Doak, R. Bruce
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons92933

Foucar, Lutz
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons117815

Hartmann, Elisabeth
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons183393

Hilpert, Mario
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons183396

Nass Kovács, Gabriela
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons183399

Roome, Christopher M.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95345

Shoeman, Robert L.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95189

Schlichting, Ilme
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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https://doi.org/10.1038/s41467-020-15610-4
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https://static-content.springer.com/esm/art%3A10.1038%2Fs41467-020-15610-4/MediaObjects/41467_2020_15610_MOESM3_ESM.pdf
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Citation

Nass, K., Gorel, A., Abdullah, M. M., Martin, A. V., Kloos, M., Marinelli, A., et al. (2020). Structural dynamics in proteins induced by and probed with X-ray free-electron laser pulses. Nature Communications, 11(1): 1814 (2020), pp. 1-9. doi:10.1038/s41467-020-15610-4.

Cite as: https://hdl.handle.net/21.11116/0000-0006-3BEA-1

Abstract

X-ray free-electron lasers (XFELs) enable crystallographic structure determination beyond the limitations imposed upon synchrotron measurements by radiation damage. The need for very short XFEL pulses is relieved through gating of Bragg diffraction by loss of crystalline order as damage progresses, but not if ionization events are spatially non-uniform due to underlying elemental distributions, as in biological samples. Indeed, correlated movements of iron and sulfur ions were observed in XFEL-irradiated ferredoxin microcrystals using unusually long pulses of 80 fs. Here, we report a femtosecond time-resolved X-ray pump/X-ray probe experiment on protein nanocrystals. We observe changes in the protein backbone and aromatic residues as well as disulfide bridges. Simulations show that the latter's correlated structural dynamics are much slower than expected for the predicted high atomic charge states due to significant impact of ion caging and plasma electron screening. This indicates that dense-environment effects can strongly affect local radiation damage-induced structural dynamics.