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  Indications of radiation damage in ferredoxin microcrystals using high-intensity X-FEL beams

Nass, K., Foucar, L., Barends, T., Hartmann, E., Botha, S., Shoeman, R. L., et al. (2015). Indications of radiation damage in ferredoxin microcrystals using high-intensity X-FEL beams. Journal of Synchrotron Radiation, 22(2), 225-238. doi:10.1107/S1600577515002349.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0026-CDE1-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0026-CDE2-A
Genre: Journal Article

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 Creators:
Nass, Karol1, Author              
Foucar, Lutz1, Author              
Barends, Thomas1, Author              
Hartmann, Elisabeth1, Author              
Botha, Sabine1, Author              
Shoeman, Robert L.1, Author              
Doak, Bruce1, Author              
Alonso-Mori, Roberto, Author
Aquila, Andrew, Author
Bajt, Sas¡a, Author
Barty, Anton, Author
Bean, Richard, Author
Beyerlein, Kenneth R., Author
Bublitz, Maike, Author
Drachmann, Nikolaj, Author
Gregersen, Jonas, Author
Jönsson, H. Olof, Author
Kabsch, Wolfgang, Author
Kassemeyer, Stephan, Author
Koglin, Jason E., Author
Krumrey, Michael, AuthorMattle, Daniel, AuthorMesserschmidt, Marc, AuthorNissen, Poul, AuthorReinhard, Linda, AuthorSitsel, Oleg, AuthorSokaras, Dimosthenis, AuthorWilliams, Garth J., AuthorHau-Riege, Stefan, AuthorTimneanu, Nicusor, AuthorCaleman, Carl, AuthorChapman, Henry N., 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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Free keywords: SFX; free-electron laser; metalloprotein; protein crystallography; radiation damage; serial femtosecond crystallography
 Abstract: Proteins that contain metal cofactors are expected to be highly radiation sensitive since the degree of X-ray absorption correlates with the presence of high-atomic-number elements and X-ray energy. To explore the effects of local damage in serial femtosecond crystallography (SFX), Clostridium ferredoxin was used as a model system. The protein contains two [4Fe-4S] clusters that serve as sensitive probes for radiation-induced electronic and structural changes. High-dose room-temperature SFX datasets were collected at the Linac Coherent Light Source of ferredoxin microcrystals. Difference electron density maps calculated from high-dose SFX and synchrotron data show peaks at the iron positions of the clusters, indicative of decrease of atomic scattering factors due to ionization. The electron density of the two [4Fe-4S] clusters differs in the FEL data, but not in the synchrotron data. Since the clusters differ in their detailed architecture, this observation is suggestive of an influence of the molecular bonding and geometry on the atomic displacement dynamics following initial photoionization. The experiments are complemented by plasma code calculations

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Language(s): eng - English
 Dates: 2014-09-252015-02-032015-02-172015-03-01
 Publication Status: Published in print
 Pages: 14
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
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Title: Journal of Synchrotron Radiation
  Abbreviation : J. Synchrotron Radiat.
Source Genre: Journal
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Publ. Info: Copenhagen, Denmark : Published for the International Union of Crystallography by Munksgaard
Pages: - Volume / Issue: 22 (2) Sequence Number: - Start / End Page: 225 - 238 Identifier: ISSN: 0909-0495
CoNE: https://pure.mpg.de/cone/journals/resource/954925562624