An ensemble of cryo-EM structures reveals how eukaryotic elongation factor 2 positions the first codon of a viral mRNA for translation.

Ensemble cryo-EM visualizes how structural rearrangements poise the newly made protein and release factor RF2 to dissociate in preparation for ribosome recycling.

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.

Correlation-driven molecular dynamics provides a fully automated and human-bias-free framework for quantitative interpretation of modern cryo-electron microscopy data.

Creating structural models with multiple conformations of proteins improves the fit of the model to experimental data X-ray crystallography and improve the model geometry.

Cryo-EM analysis of full-length human epidermal growth factor receptor provides a molecular explanation for how ligand-induced differential effect in the ligand-binding extracellular module tunes the transmembrane signaling mediated by epidermal growth factor receptor.

Cryo-EM structures capture different conformational states of chromatin remodeler-nucleosome complexes.

Conformation-specific nanobodies enable to capture and solve the first GTP-bound active structure of a bacterial homolog of the Parkinson-associated LRRK2 protein, providing insights into the activation mechanism of these proteins.

Extensive benchmarking reveals that errors made when manually building models into near-atomic-resolution cryoEM density may automatically be corrected using an improved Rosetta-based structure refinement method.

Structural insights show how RNA chaperones cooperate to recognise defined target transcripts and suppress gene expression.