The ability of lipid nanodiscs to trap different types of amyloid intermediates, as successfully demonstrated in this study for human-IAPP, could become one of the most powerful approaches to dissect the complicated misfolding pathways of protein aggregation.

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.

Unprecedented resolution of the molecular mechanisms of plant membrane protein anchoring involving phospholipids and sterols reveals the control of spatio-temporal segregation into plasma membrane nanodomains.

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.

Lipids with a propensity to form nonbilayer structures must be present for the last step of membrane fusion to take place.

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.

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.

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

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