Florian Dworkowski

This paper resolves the mechanism of covalent bond formation in a LOV photoreceptor using time-resolved crystallography and spectroscopy, revealing a water-mediated proton transfer that accelerates the reaction by fourteen orders of magnitude.

The paper elucidates the structural basis of the two-photon photoactivation mechanism of orange carotenoid protein using a combination of structural and biochemical methods.

This study uses time-resolved crystallography and MD simulations to reveal structural changes in C1C2 channelrhodopsin during activation, showing how conformational shifts enable ion conduction.

This paper reports a method to capture the blue-light activated state of the Phot-LOV1 domain using time-resolved serial synchrotron crystallography and provides structural insights into its activation cascade.

The paper validates a fixed-target delivery system for XFEL crystallography, showing reduced sample consumption and light contamination control for light-sensitive proteins.

The paper captures the release of a photopharmacological drug from tubulin using time-resolved serial crystallography and shows how ligand release triggers conformational changes.