Mining electron cryomicroscopy data reveals new ribosomal interactions that preclude translation to potentially regulate gene expression.

The high-resolution structure of a filamentous flexible plant virus shows that there is structural homology between its coat protein and the nucleoproteins of an unrelated group of enveloped RNA animal viruses.

The structure of the Mycobacterium smegmatis CIII₂CIV₂ respiratory supercomplex with telacebec (Q203) bound shows how this tuberculosis drug candidate blocks respiration in mycobacteria.

The architecture of the bacterial cytokinetic ring in cells and in artificial liposome reconstitutions has been described using electron microscopy, leading to a mechanism of constriction.

Electron-cryomicroscopy structures of the supercomplex of NSF, αSNAP, and neuronal SNAREs in the presence of ATP under non-hydrolyzing conditions at 3.9 Å resolution reveal interactions between the N-terminal residues of SNAP-25 and NSF.

Live-cell imaging, genetic analysis and electron cryomicroscopy identify structural motifs involved in the differential assembly of Pol I-Rrn3 complexes and Pol I homodimers in response to nutrient availability.

The structure of a substrate-engaged AAA+ unfoldase suggests a model for processive unfolding that is supported by biochemical data.

Cryo-EM and particle classification techniques reveal how the electron-bifurcating [FeFe] hydrogenase from Thermotoga maritima multimerizes to connect distant active sites and reveal different conformational states that enable catalysis.

Structural analysis of the ATP synthase – in combination with evolutionary covariance analysis – reveals the fold of the a subunit and shows that the enzyme can adopt several different conformations, which support the Brownian ratchet model for generating rotation.