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.

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

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.

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

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

The nature of the phycobilisome–photosystem II supercomplex on the native thylakoid determined with cryo-electron tomography at an unprecedented resolution reveals that one phycobilisome interconnects with six photosystem monomers.

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.

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

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

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.