The structure of a large enzyme complex involved in methanogenesis was determined at high resolution by electron cryo-microscopy.

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.

The atomic model of a mitochondrial ATP synthase dimer underlies functions of its specific protein constituents and boundary cardiolipins.

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.

Two cryo-EM structures of the mammalian BBSome show how the BBSome is recruited to membranes and activated by the GTPase ARL6 prior to binding transmembrane proteins.

Construction of a first atomic model for an intact bacterial ATP synthase allows for a structural understanding of the roles of individual amino acids in the mechanism of ATP synthesis.

Cryo-EM reveals how the central functional site of the ribosome is assembled and provides a framework to interpret the consequences of mutations linked to leukaemia-associated ribosomopathies.

New functionality in RELION-4.0 allows convenient structure determination from cryo electron tomography data to resolutions sufficient for de novo atomic modelling.

Assembly of the human enzyme inosine monophosphate dehydrogenase 2 into filaments promotes substrate-dependent resistance to feedback inhibition by downstream products, promoting increased flux during proliferative states.

High resolution SthK channel cryo-EM structures in different ligand-bound states combined with single-channel functional data in the same conditions constrain a gating mechanism for CNG channels.