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The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography

Journal Article · · Scientific Reports
DOI:https://doi.org/10.1038/srep35279· OSTI ID:1348400
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  1. Univ. of Gothenburg, Gothenburg (Sweden)
  2. Univ. of Gothenburg, Gothenburg (Sweden); Univ. of Jyvaskyla, Jyvaskyla (Finland); Univ. of Helsinki, Helsinki (Finland)
  3. Univ. of Jyvaskyla, Jyvaskyla (Finland)
  4. Deutsches Elektronen-Synchrotron (DESY), Hamburg (Germany)
  5. The Univ. of Tokyo, Tokyo (Japan)
  6. Arizona State Univ., Tempe, AZ (United States)
  7. LaTrobe Univ., Melbourne, VIC (Australia)
  8. Univ. of Wisconsin, Milwaukee, WI (United States)
  9. SLAC National Accelerator Lab., Menlo Park, CA (United States)
  10. RIKEN SPring-8 Center, Hyogo (Japan)
  11. Univ. of Chicago, Chicago, IL (United States); Argonne National Lab. (ANL), Argonne, IL (United States)
  12. Northern Illinois Univ., Chicago, IL (United States)
+ Show Author Affiliations

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 Å 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 Å 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. As a result, the study paves the way for time-resolved structural investigations of the phytochrome photocycle with time-resolved SFX.

Research Organization:
SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)
Sponsoring Organization:
USDOE
Grant/Contract Number:
AC02-76SF00515
OSTI ID:
1348400
Journal Information:
Scientific Reports, Journal Name: Scientific Reports Journal Issue: 1 Vol. 6; ISSN 2045-2322
Publisher:
Nature Publishing GroupCopyright Statement
Country of Publication:
United States
Language:
English

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Cited By (9)

The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography dataset October 2016
Drop-on-demand sample delivery for studying biocatalysts in action at X-ray free-electron lasers journal February 2017
Hydroxyethyl cellulose matrix applied to serial crystallography journal April 2017
Viscosity-adjustable grease matrices for serial nanocrystallography journal January 2020
Microfluidics: From crystallization to serial time-resolved crystallography journal May 2017
On the (un)coupling of the chromophore, tongue interactions, and overall conformation in a bacterial phytochrome journal April 2018
Non-cryogenic structure of a chloride pump provides crucial clues to temperature-dependent channel transport efficiency journal November 2018
Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome journal August 2018
Sample delivery for serial crystallography at free-electron lasers and synchrotrons journal January 2019

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59 BASIC BIOLOGICAL SCIENCES
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