Journal
SCIENTIFIC REPORTS
Volume 6, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/srep35279
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Funding
- European Research Council
- Foundation of Strategic Research, Sweden
- National Science Foundation (NSF) MCB grant [1413360]
- Academy of Finland
- Finnish Cultural Foundation
- Foundation of International Cooperation in Research and Higher Education, Sweden (STINT)
- X-ray Free Electron Laser Priority Strategy Program (MEXT, Japan)
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- NIH [P41GM103393]
- CFEL DESY through program-oriented funds of the Helmholtz Association
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1413360] Funding Source: National Science Foundation
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Phytochromes are a family of photoreceptors that control light responses of plants, fungi and bacteria. A sequence of structural changes, which is not yet fully understood, leads to activation of an output domain. Time-resolved serial femtosecond crystallography (SFX) can potentially shine light on these conformational changes. Here we report the room temperature crystal structure of the chromophore-binding domains of the Deinococcus radiodurans phytochrome at 2.1 angstrom resolution. The structure was obtained by serial femtosecond X-ray crystallography from microcrystals at an X-ray free electron laser. We find overall good agreement compared to a crystal structure at 1.35 angstrom resolution derived from conventional crystallography at cryogenic temperatures, which we also report here. The thioether linkage between chromophore and protein is subject to positional ambiguity at the synchrotron, but is fully resolved with SFX. The study paves the way for time-resolved structural investigations of the phytochrome photocycle with time-resolved SFX.
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