Within the isolated lid sub-complex of the proteasome, a finely tuned network of interactions maintains the deubiquitinase in an inhibited conformation; dramatic rearrangements of the lid subunits upon incorporation into the holoenzyme lead to the deubiquitinase’s activation.

Water molecules and amino-acid side chain rotamers have been resolved in the cryoEM structure of T20S proteasome at 2.8 angstroms.

Empirical energy landscape allows simulating the structural dynamics of the proteasomal ATPase complex, which yields predictions that are widely consistent with experimental observations and reveals the functional mechanism of the proteasome in substrate degradation.

The Volta phase plate enables in-focus single particle analysis at near atomic resolutions, which could expand the capabilities of cryo-EM, especially for small, flexible or heterogeneous macromolecular samples.

Local sharpening of cryo-electron microscopy maps using atomic models can increase the interpretability of densities in cases of resolution variation and facilitates model building and refinement.

New hybrid structure determination methods leveraging the inherent biophysical properties of a macromolecule through molecular dynamics simulations provide accurate and cost-efficient ways of achieving atomic structures from high resolution cryo-electron density maps.

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

Experimental and computational analyses reveal how proteasomal hydrolysis is regulated and show that peptide transport is the rate-limiting step and the main differentiating factor between human standard- and immuno-proteasomes.

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

Proteasomes are protected from autophagic elimination upon carbon starvation by sequestration into cytoplasmic storage granules, which aid cell fitness by providing a cache of proteasomes that can be rapidly remobilized when carbon availability improves.