Advances in imaging techniques have shed new light on the structure of vesicles formed by COPI protein complexes.

A molecular model of the assembled COPI coat, determined by cryo-electron tomography of an in vitro reconstituted budding reaction, reveals details of interactions mediating coat assembly and shows the binding site of ArfGAP2.

Electron cryo-tomography reveals a huge conformational change in the secretin domain of the type IV pilus machinery that occurs when the channel opens for pilus extrusion.

A detailed description of the structure of procentriole MT triplet by cryoET, along with its associated non-tubulin proteins and its assembly intermediates, reveals possible molecular mechanism for the procentriole assembly.

Cryo-electron tomography of COPI vesicles in the Golgi reveals coat structure, disassembly dynamics, cargo binding, and morphological variability.

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

Hydrophilized graphene prevents protein denaturation at the air-water interface.

Imaging with electron microscopy and cryo-electron tomography reveals that competition between Cdc42 and Gic1 for the same subunit within septins controls the formation and breakdown of septin filaments.

In situ cryo-electron tomography resolves individual photosynthetic complexes within native thylakoid membranes, revealing how thylakoid architecture sorts proteins into discrete membrane domains.

The automation of cryo-focused ion beam milling enables previously unfeasible cryo-electron tomography projects.