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

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: 1814 (2020), pp. 1-9. doi:10.1038/s41467-020-15610-4.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0006-3BEA-1 Version Permalink: http://hdl.handle.net/21.11116/0000-0006-3BEB-0
Genre: Journal Article

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 Creators:
Nass, Karol1, Author              
Gorel, Alexander1, Author              
Abdullah, Malik M., Author
Martin, Andrew V., Author
Kloos, Marco1, Author              
Marinelli, Agostino, Author
Aquila, Andrew, Author
Barends, Thomas R. M.1, Author              
Decker, Franz-Josef, Author
Doak, R. Bruce1, Author              
Foucar, Lutz1, Author              
Hartmann, Elisabeth1, Author              
Hilpert, Mario1, Author              
Hunter, Mark S., Author
Jurek, Zoltan, Author
Koglin, Jason E., Author
Kozlov, Alexander, Author
Lutman, Alberto A., Author
Nass Kovács, Gabriela1, Author              
Roome, Christopher M.1, Author              
Shoeman, Robert L.1, Author              Santra, Robin, AuthorQuiney, Harry M., AuthorZiaja, Beata, AuthorBoutet, Sébastien, AuthorSchlichting, Ilme1, Author               more..
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 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.

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Language(s): eng - English
 Dates: 2020-04-14
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 11 Sequence Number: 1814 (2020) Start / End Page: 1 - 9 Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723