ArticleScientific reports2016
The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 51 citations in OpenAlex.
- A simple and practical approach for protein serial crystallography using grease matrix and large-area support film.Journal of synchrotron radiation · 2026Article
- Proton-Coupled Chromophore and Protein Structural Changes Control Phytochrome Activation.Biochemistry · 2026Article
- Time-resolved small-angle X-ray scattering system development for the biological macromolecules at SACLA: A pilot study.Biophysics and physicobiology · 2025Article
- Photoreception and signaling in bacterial phytochrome revealed by single-particle cryo-EM.Science advances · 2024Article
- Blue and red in the protein world: Photoactive yellow protein and phytochromes as revealed by time-resolved crystallography.Structural dynamics (Melville, N.Y.) · 2024Article
- Review of serial femtosecond crystallography including the COVID-19 pandemic impact and future outlook.Structure (London, England : 1993) · 2023Review
- Vibrational Spectroscopy of Phytochromes.Biomolecules · 2023Review
- Conserved histidine and tyrosine determine spectral responses through the water network in Deinococcus radiodurans phytochrome.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022Article
- Enhancing the Inhomogeneous Photodynamics of Canonical Bacteriophytochrome.The journal of physical chemistry. B · 2022Article
- Dynamic Structural Biology Experiments at XFEL or Synchrotron Sources.Methods in molecular biology (Clifton, N.J.) · 2021Review
- The primary structural photoresponse of phytochrome proteins captured by a femtosecond X-ray laser.eLife · 2020Article
- Viscosity-adjustable grease matrices for serial nanocrystallography.Scientific reports · 2020Article
- Modulation of Structural Heterogeneity Controls Phytochrome Photoswitching.Biophysical journal · 2020Article
- High-viscosity sample-injection device for serial femtosecond crystallography at atmospheric pressure.Journal of applied crystallography · 2019Article
- Macromolecular Nanocrystal Structural Analysis with Electron and X-Rays: A Comparative Review.Molecules (Basel, Switzerland) · 2019Review
- Time-Resolved Macromolecular Crystallography at Pulsed X-ray Sources.International journal of molecular sciences · 2019Review
- Sample delivery for serial crystallography at free-electron lasers and synchrotrons.Acta crystallographica. Section D, Structural biology · 2019Review
- Non-cryogenic structure of a chloride pump provides crucial clues to temperature-dependent channel transport efficiency.The Journal of biological chemistry · 2019Article
- Article
- On the (un)coupling of the chromophore, tongue interactions, and overall conformation in a bacterial phytochrome.The Journal of biological chemistry · 2018Article
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36 authors at 14 institutions in 6 countries.
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Abstract
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. The study paves the way for time-resolved structural investigations of the phytochrome photocycle with time-resolved SFX.
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