PSI researchers have developed a new method to attach proteins to the surface of virus-like particles.
Scientists decode the structure of the enzyme responsible for the ethane fixation by – beside others – using the SLS.
Crystal structure of SARS-CoV-2 Orf9b in complex with human TOM70 suggests unusual virus-host interactions
In a study published in Nature Communications, researchers at the NHC Key Laboratory of Systems Biology of Pathogens in Beijing, China, in collaboration with the Paul Scherrer Institut characterize the interactions of SARS-CoV-2 orf9b and human TOM70 biochemically, and they determine the 2.2 Å crystal structure of the TOM70 cytosolic domain with a bound SARS-CoV-2 orf9b peptide.
Researchers at Goethe University Frankfurt, in cooperation with the PSI have probably discovered another, previously unknown mechanism of action of the antiviral remdesivir.
In a study addressing the global health threat of drug resistance, researchers at the Biozentrum, University of Basel, have revealed how a new antibiotic, Darobactin, binds to the external membrane of gram-negative bacteria.
The Dikic group at the Goethe University in Frankfurt am Main, Germany has published the first results following the opening of the "PRIORITY COVID-19 Call” at SLS.
In the week of April 1-5 PSI welcomes 20 PhD students and postdocs taking part in the European HERCULES 2019 school on Neutron and Synchrotron Radiation. They will attend lectures and perform two days of practical courses at several beam lines of the Swiss Light Source.
Fast and accurate data collection for macromolecular crystallography using the JUNGFRAU detector.
On the 7th to 12th of August 2018, a collaborative group of scientists from the Paul Scherrer Institute and members of the LeadXpro and Heptares pharmaceutical companies led by Karol Nass (PSI macromolecular crystallography MX-SLS group) performed the first serial femtosecond crystallography (SFX) pilot user experiment at the SwissFEL X-ray free electron laser (XFEL).