Przemysław Nogły

This paper establishes a robust workflow for injector-based pump-probe TR-SSX at the MicroMAX beamline to study CrPhotLOV1 structural dynamics.

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

This paper uses time-resolved crystallography to visualize how light activates Rac1 by tilting the LOV2 domain and partially opening switch I when GDP-bound.

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.

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.