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

Cryo electron tomography provides the first high-resolution 3D axoneme structure from any pathogenic organism, revealing novel structures that support the unique motility of these pathogens through host tissues.

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.

Tubulin engages unique lateral interactions without longitudinal ones during microtubule polymerization, leaving holes of a few subunits size potentially at the origin of tubulin exchange within their shaft.

An atomic model of the bacterial chemosensory array obtained through the synthesis of cryo-electron tomography and large-scale molecular-dynamics simulations reveals a new kinase conformation during signaling events.

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

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

The integration of structural data from different imaging scales requires the development of standards and tools for representing the segmentation and transformation of data, and for the annotation of biological structures.

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.

Rapid, label-free, volumetric, and automated assessment of the immunological synapse dynamics is demonstrated by combining optical diffraction tomography and deep-learning-based segmentation, providing a new option for immunological research.