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

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.

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.

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

The crystal structure of bacterial RNA polymerase bound to the transcription bubble reveals key features that support the formation of a double-strand/single-strand DNA junction at the upstream edge of the −10 element where bubble formation initiates.

The crystal structure of Pur-alpha in complex with DNA reveals its molecular mechanisms of nucleic-acid binding and unwinding, allowing for a better understanding of its essential role in neurons.

A dopamine transporter deficiency syndrome (DTDS)-linked mutation, R445C, underlies dopamine dysfunction and, more broadly, the clinical phenotypes shared by DTDS and Parkinson’s disease.

Experimental determination of residue contacts from mutational data allows model discrimination and identification of in vivo functional conformations of proteins.

X-ray crystallography reveals how kinesin-1 recognises a novel class of cargo adaptor motifs in an isoform-specific manner.

Structural analysis reveals large-scale conformational changes in the active site metallocluster of a CO2-fixing enzyme.