A new electron diffraction technique called MicroED allows protein structures to be determined from three-dimensional microcrystals.

A combination of molecular dynamics simulations and X-ray diffraction data has been used to construct more realistic models of proteins and to provide new insights into their interactions with other proteins and biomolecules.

Creating structural models with multiple conformations of proteins improves the fit of the model to experimental data X-ray crystallography and improve the model geometry.

Many small-molecule fragments bind differently to the allosteric protein PTP1B in room-temperature instead of cryogenic crystal structures, which may be relevant for structure-based drug design.

A combination of simulations and experiments was used to discover druggable cryptic pockets in non-structural protein 1, a promising but difficult target for coronaviruses, indicating a viable drug discovery approach for otherwise undruggable targets.

Time-resolved crystallography provides insight into the photochemical reactions in photoreceptor proteins, explaining the earliest steps of how plants, fungi and bacteria sense red light.

Time-resolved serial femtosecond crystallography revealed retinal kink and early changes in channelrhodopsin, which leads to the ion pore formation.

The conformations of the enzyme cyclophilin A that are essential for its catalytic activity are temperature dependent and exhibit diverse responses, which is consistent with a complex energy landscape.

The c-terminus of PI3K plays a key role in regulating kinase activity, with c-terminal disease-linked mutations leading to either activation or inhibition, which reveal a path to specific inhibitors.

By measuring how multiple conformations shift in response to temperature, a new allosteric binding site is discovered for the phosphatase PTP1B.