L. Gelisio

The paper demonstrates the first X-ray diffraction pattern from a single protein, Escherichia coli GroEL, showing the feasibility of ultrafast imaging of single proteins.

This study identifies three natural compounds that inhibit SARS-CoV-2 PLpro by binding to the ISG15/Ub-S2 allosteric site, showing antiviral activity and potential for drug design.

This paper determines the structure of Tpp49Aa1 using MHz-SFX and investigates its interaction with Cry48Aa1, expanding its known target range to include additional mosquito species.

The paper directly observes fast ligand binding in a biomedically relevant enzyme using MHz X-ray pulses at the European XFEL.

The paper identifies 37 compounds binding to SARS-CoV-2 main protease through X-ray crystallography, with five non-peptidic compounds showing antiviral activity in cell-based assays.

The paper presents the crystal structure of SARS-CoV-2 main protease covalently bound to a metabolite of HEAT, revealing a pro-drug mechanism and potential for non-peptidic inhibitors.