Electron cryo-microscopy has been used to determine the structure of Chikungunya virus-like particles and to provide new insights into their interactions with four different antibodies.

Structural analysis of an AKAP18-protein kinase A complex reveals that regions of intrinsic disorder impact the phosphorylation of preferred substrates.

A conserved viral protein complex that promotes membrane wrapping of nascent herpesvirus particles shows structural similarity to cellular membrane-remodelling proteins, suggesting functional mimicry.

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

New functionality in RELION-4.0 allows convenient structure determination from cryo electron tomography data to resolutions sufficient for de novo atomic modelling.

Co-evolving residue pairs in the different components of a protein complex almost always make contact across the protein–protein interface, thus providing powerful restraints for the modeling of protein complexes.

Building on previous work (Uervirojnangkoorn et al., 2015), we demonstrate how improved methods for processing XFEL diffraction data enable the determination of structures from poorly diffracting crystals.

Cryo-electron microscopy reveals interactions at the interface between adeno-associated virus and its cellular receptor at 2.4Å resolution.

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.

Analysis of the Escherichia coli DnaB helicase•bacteriophage λ helicase loader (λP) complex provides insights into helicase opening, delivery to the origin and ssDNA entry, and closing in preparation for translocation.