Guillaume Gotthard

The paper reports room-temperature light-state structures of AsLOV2-Rac1 using serial femtosecond crystallography, revealing structural changes upon light activation.

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.

The paper describes the photoactivation mechanism of the B12 photoreceptor CarH using structural and spectroscopic methods, revealing unique intermediates that drive tetramer dissociation.

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.