Westenhoff Group

Time resolved structural biology of photoactive proteins
The aim of our research is to understand structural dynamics of biological photoactive systems. Time-resolved crystallography allows us to make molecular movies of photoactive systems transiting between their illuminated and non-illuminated states. This allows us to identify how the conformational changes in proteins occur and which molecules are participating in the dynamics. Combining the results from the other topics with SFX data allows us to increase our knowledge of how photoactive proteins work on a molecular level.
Group members
Publications
Time-resolved serial crystallography to reveal protein structural changes
Part of Trends in Biochemical Sciences (TIBS), p. 183-184, 2024
- DOI for Time-resolved serial crystallography to reveal protein structural changes
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Part of Nature Chemistry, p. 624-632, 2024
- DOI for Directed ultrafast conformational changes accompany electron transfer in a photolyase as resolved by serial crystallography
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Part of Nature Methods, p. 1608-1611, 2024
- DOI for Microsecond time-resolved X-ray scattering by utilizing MHz repetition rate at second-generation XFELs
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Part of Structure, p. 1952-1962000, 2024
- DOI for Cryo-EM structures of a bathy phytochrome histidine kinase reveal a unique light-dependent activation mechanism
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Part of Journal of Chemical Physics, 2023
- DOI for Ground-state heterogeneity and vibrational energy redistribution in bacterial phytochrome observed with femtosecond 2D IR spectroscopy
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3D-printed sheet jet for stable megahertz liquid sample delivery at X-ray free-electron lasers
Part of IUCrJ, p. 662-670, 2023
- DOI for 3D-printed sheet jet for stable megahertz liquid sample delivery at X-ray free-electron lasers
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Structural basis of the radical pair state in photolyases and cryptochromes
Part of Chemical Communications, p. 4889-4892, 2022
- DOI for Structural basis of the radical pair state in photolyases and cryptochromes
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Structural mechanism of signal transduction in a phytochrome histidine kinase
Part of Nature Communications, 2022
- DOI for Structural mechanism of signal transduction in a phytochrome histidine kinase
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Part of Current opinion in structural biology, 2022
- DOI for Protein motions visualized by femtosecond time-resolved crystallography: The case of photosensory vs photosynthetic proteins
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