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.

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.

The corkscrew-like motility of Spirochete bacteria is enabled by a unique, asymmetrically constructed flagellum that wraps around the cell body within the periplasm.