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

Visualization of yeast spindle pole proteins using a new microscopy method shows that assembly into the nuclear membrane occurs at the same time as duplication.

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

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

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.

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.

Direct estimation of the Hurst exponent shows that endosomes and lysosomes reside in regimes of persistent and anti-persistent motion with heavy-tailed residence time distributions and motion correlated with endocytic function.

The structure of KvAP addresses a mechanism of voltage-dependent gating that has been debated for 16 years.

Cryo-EM structures reveal how the peptidisc scaffold can adapt to different membrane proteins, establishing it as a universal membrane mimetic to stabilize membrane proteins in solution.

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