In an article at BioRxiv, Daniel A. Keedy et al. perform two RT (room temperature) crystallographic screens, single-crystal and in-situ, of PTP1B using many of the same fragments from an earlier cryo crystallographic screen of PTP1B. This RT screen represents "the largest RT crystallography screens of a diverse library of ligands to date, and enabling a direct interrogation of the effect of data collection temperature on protein-ligand interactions."
"Their main findings suggests that the vast body of existing cryogenic-temperature protein-ligand structures may provide an incomplete picture, and highlights the potential of RT crystallography to help complete this picture by revealing distinct conformational modes of protein-ligand systems. Our results may inspire future use of RT crystallography to interrogate the roles of protein-ligand conformational ensembles in biological function."
Our MiTeGen In Situ-1 crystallography plates were used in this research.