Multi-body refinement in RELION allows high-resolution reconstruction and visualisation of molecular motions in cryo-EM single-particle data sets with continuous forms of structural heterogeneity.

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.

The dynamic structure of respiratory complex I from mesophilic bacterium is revealed and demonstrates existence of uncoupled conformations in the bacterial complex.

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

Cryo-EM reveals that an unexpected domain separation in the zona pellucida module of uromodulin is required for its assembly to filamentous homopolymers that promote pathogen clearance in urinary tract infections.

Cryo-EM studies reveal structural basis for the activation, auto-inhibition and regulation of RET receptor tyrosine kinase.

The structures of plant CIII2, CIV, and SC III2+IV challenge long-standing assumptions, generate new mechanistic hypotheses and allow for the generation of more selective agricultural inhibitors.

Structural and biochemical studies indicate that AAA+ ATPase employ a general mechanism to translocate a variety of substrates, including extended polypeptides, hairpins, crosslinked chains, and chains conjugated to other molecules.

A masked cryo-EM image classification approach and the structure of an inhibitor-bound complex provide insights into the molecular flexibility of the catalytic subunit of gamma-secretase.

High-resolution maps and models of the bacterial ribosome provide new chemical insights into protein synthesis, and should enable the development of robust tools for cryo-EM structure modeling and refinement.