Fiducial-less tomography on single particle cryoEM samples reveals that most particles are adsorbed to the air-water interface and allows for researchers to diagnose and solve sample, grid, ice thickness, collection, and processing issues.

New functionality in RELION-4.0 allows convenient structure determination from cryo electron tomography data to resolutions sufficient for de novo atomic modelling.

Cryo-electron tomography reveals how a chaperone protein called TRiC reduces the ability of pathogenic mutant huntingtin proteins to form aggregates.

CryoEM reveals the structure of a two-component archaeal S-layer, which sheds new light on archaeal cell biology.

The resolution of electron cryo-microscopy can be improved by using optimal exposure values to filter video frames.

Using both electron cryo-tomography and helical reconstruction, the first structure of the entire archaellum machinery with an assembled filament has been determined, providing the structural basis for our understanding of archaeal motility.

The surface layer of Sulfolobus acidocaldarius consists of a flexible but stable outer protein layer that interacts with an inner, membrane-bound protein.

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

CTFFIND5 estimates the thickness and tilt of cryogenic electron microscopy samples directly from the power spectrum of a single exposure.

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