A combination of direct-electron detectors and statistical movie processing allows ribosome cryo-EM structures to be determined to resolutions that were previously only attainable by X-ray crystallography.

Cryo-electron microscopy has been used to provide a structural interpretation of the complete action cycle of release factor 3 during translation termination, which includes a coordinated sequence of interactions with a class-I release factor and the ribosome.

A novel strategy for reproducible cryo-EM sample preparation with minimal sample volumes.

Using GPUs for the costly computations in cryo-EM enables structure determination in mere days on a single workstation.

The identification of the insulin binding site 2 by high resolution cryo-EM analysis.

Cryo-EM studies reveal that incubation with ATP produces conformational intermediates of E. coli ATP synthase, in which the ε subunit is no longer in its autoinhibitory conformation.

Cryo-EM analysis of human ZnT8 reveals a large conformational change of TMD during the transport cycle.

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

The cryo-EM structure and functional characterization of the chloride-selective ion transporter Slc26a9 defines its oligomeric architecture and transport mechanism.

Cryo-EM structure of monomeric human Frizzled5 was determined with a universal fiducial antibody at 3.7 Å overall resolution, which supports a simple Fzd/LRP6 heterodimerization mechanism of canonical Wnt/β-catenin signaling.