Post-refinement methods enable the use of X-ray free electron lasers for biological crystallography of systems in which sample quantity is a limitation.

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.

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.

Crystallography and single particle cryo-EM reveal hexameric and pentameric structures of the ExbBD energizer in the Ton system and oligomeric transition, which provides a unique working mechanism and a new vision of dynamic membrane biology.

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.

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

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

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

The inward-open and outward-open structures of MjNhaP1 explain the mechanism of electroneutral sodium-proton antiport across the cell membrane.