A structure of the complete, membrane bound, COPII coat solved by sub-tomogram averaging reveals the arrangement of all protein subunits on the membrane and suggests a mechanism for coating heterogeneously-shaped carriers.

The crystal structure of a ternary complex of a TonB-dependent transporter containing a signalling domain, bound to siderophore as well as TonB, provides mechanistic insights into siderophore uptake and signalling.

A cryo-EM structure combined with bioinformatics provide a structural view on a conserved co-translational membrane protein biogenesis pathway.

The structure of gp41with its membrane anchors highlights the flexible linkage of the transmembrane regions and the fuson peptides, which generates an asymmetric conformation, a potential target of MPER bNAbs.

The structure of a bivalent double-knot tarantula toxin bound to the outer pore of the capsaicin receptor reveals a novel mode of toxin-channel recognition that has important implications for thermosensation.

Snf7 crystal structures reveal the mechanisms of ESCRT-III activation and polymerization into membrane-remodeling filaments.

A newly discovered membrane structure associates with one of the centrioles and affects two important centrosomal events in epidermal cells – ciliary positioning and spindle orientation – through a physical interaction.

GTP binding induces rearrangement of S-OPA1 assembly on membrane and thus triggers membrane remodeling with reduced curvature.

The crystal structure of human WIPI2 bound to the ATG16L1 WIPI2-interacting region, combined with in vitro reconstitution and cellular autophagy assays, shows how the LC3 lipidation machinery is recruited in autophagy initiation.

The near-atomic cryoEM pore complex structure of pneumolysin, the main virulence factor of Streptococcus pneumoniae, shows how the individual domains rearrange during the pore formation.