Protein disaggregases employ two mechanically-linked ATPase rings that are under steric control by a wrapped-around coiled-coil belt.

The structure of the entire Mot1 Swi2/Snf2 protein uncovers an unexpected auto-inhibited resting state activated by substrate binding, and suggests a DNA pulling mechanism of TBP displacement.

Bacterial CRISPR immunity tracks phage mutations, creating immune diversity in bacterial populations that parallels phage genetic diversity and patterns of phage evolution that are determined by the type and degree of immune cross-reactivity in the CRISPR system.

The site of ubiquinone binding observed in the cryo-EM structure of respiratory complex I during turnover supports a two-state stabilization change mechanism.

The structure of the yeast HOPS tethering complex suggests how this large complex may catalyze fusion by tethering Rab-decorated membranes and promoting the assembly of SNAREs.

Electron cryo-tomography reveals a huge conformational change in the secretin domain of the type IV pilus machinery that occurs when the channel opens for pilus extrusion.

The structural and functional analysis of the ATP-dependent RNA helicase Prp43 provides insights into the mechanisms of RNA binding and translocation, which could serve as paradigm for all DEAH-box proteins.

Whereas in a paradigmatic structure an SM protein chaperone clamps its client SNARE shut, a second structure demonstrates that an SM protein can also hold its SNARE open to promote assembly.

A multidimensional chemical mapping strategy enables confident determination of the structures of non-coding RNAs at 1-nm resolution, including previously intractable riboswitch and human regulon states.

The intracellular network that distributes iron-sulfur clusters in bacteria is surprisingly 'plug and play' with iron-sulfur enzymes acquired from distantly related species, whereas the intracellular electron transfer network often needs plug adapters to connect with foreign enzymes.