Prof. Dr. Jörg Standfuss

Jörg Standfuss was born in Germany and trained in structural biology and biophysics. He earned his Ph.D. at the Max Planck Institute for Biophysics and the University of Frankfurt, where he determined the structure of the major light-harvesting complex II, a key protein involved in photosynthetic energy capture. He then received EMBO and Marie Curie Fellowships to pursue postdoctoral research at the MRC Laboratory of Molecular Biology in Cambridge, UK. There, he used constitutively active mutants of visual rhodopsin to determine some of the earliest structures of an active G protein-coupled receptor (GPCR).
In 2010, he joined the Paul Scherrer Institute (PSI) in Switzerland, where his team pioneered pump–probe serial crystallography at the Swiss Light Source (SLS) and the Swiss X-ray Free Electron Laser (SwissFEL). His research has focused on light-driven ion and proton pumps, GPCR activation, and the photopharmacological control of proteins. His work enabled comprehensive time-resolved structural studies of retinal-binding proteins, revealing how light-induced conformational changes drive protein function on femtosecond-to-millisecond timescales. More recently, his team established the use of photopharmacological compounds as triggers in time-resolved structural biology, resolving drug release from tubulin across fourteen orders of magnitude in time.
Since 2024, he has led the Laboratory for Biomolecular Research at PSI, with the aim of firmly establishing time-resolved methods in structural biology. Since 2021 he was teaching in the Department of Biochemistry at the University of Zurich and in July 2025, he changed as Associate Professor into the Department of Chemistry. His research group continues to investigate fundamental mechanisms of biomolecular structure and function, combining advanced X-ray methods, light-activated proteins, and photopharmacology. At the University of Zurich, he contributes to teaching and graduate supervision, integrating chemistry and biophysics with time-resolved structural biology.