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.

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

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.

Nuclear pores assemble asymmetrically, by an inside-out evagination of the inner nuclear membrane that grows in diameter and depth until it fuses with the flat outer nuclear membrane.

Cryo-electron tomography unveils striking new structural components of positive-strand virus RNA replication compartments, greatly advancing mechanistic insights into the structure, assembly, function and control of these critical complexes.

The transmembrane shape of the F₁F_o ATP synthase monomer provides the molecular basis of high curvature at the ridges of mammalian mitochondrial cristae.

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.

Zebrafish genetics and cryo-electron tomography reveal distinct roles of all vertebrate PIH family proteins in axonemal dynein assembly and cilia/flagella motions, assigning specific dynein subtypes to each PIH protein.