期刊
JOURNAL OF SYNCHROTRON RADIATION
卷 22, 期 -, 页码 225-238出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1600577515002349
关键词
free-electron laser; SFX; serial femtosecond crystallography; radiation damage; protein crystallography; metalloprotein
资金
- LCLS Ultrafast Science Instruments (LUSI) - US Department of Energy, Office of Basic Energy Sciences
- Max Planck Society
- Human Frontier Science Program (HFSP)
- Swedish Research Foundation for Strategic Research
- Swedish Research Foundation
- Swedish Research Council via the Rontgen-Angstrom Cluster
- Swedish National Infrastructure for Computing (SNIC) through Uppsala Multidisciplinary Center for Advanced Computational Science (UPPMAX) [p2012227, p2013175]
- Novo Nordisk Fonden [NNF12OC0002082] Funding Source: researchfish
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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