J. Standfuss

This paper computationally designs light-responsive proteins that undergo conformational changes upon light activation, enabling precise control of biological functions.

TorchRef provides a PyTorch framework for crystallographic refinement, offering GPU acceleration and modular design for developing new refinement protocols.

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 presents the first X-ray structure of an NtA-mediated asymmetric BRAF dimer bound to MEK1, showing it is a catalytically active state, not an intermediate in BRAF activation.

This study captures time-resolved structures of β2AR modulated by a photoswitchable beta-blocker, revealing conformational changes linked to ligand isomerization and receptor function.

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