The bacterial AAA+ chaperone ClpL recognizes aggregated proteins via multiple contacts of its unique N-terminal domain and refolds them with high efficiency providing superior heat resistance.

Genetic, biochemical, and bioinformatic analyses reveal how expanding metabolic repertoire interferes with fundamental processes like protein synthesis inside cells and the role of D-aminoacyl-tRNA deacylase2 in protecting these processes during terrestrialisation.

Surveying Mycobacterium tuberculosis tRNA modification leads to identification of a modification promoting Mtb pathogenesis.

The helical cell shape of Helicobacter pylori depends on the polymerizing cytoskeletal protein CcmA’s recruitment to the cell envelope by Csd5 and CcmA’s indirect stabilization of a periplasmic cell wall hydrolase via interactions with the transmembrane protein Csd7.

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.

Cryogenic super-resolution microscopy resolves the three-dimensional arrangement of individual fluorescent markers attached to protein complexes with Angstrom precision through their blinking behavior, polarization selection and a classification scheme.

Multiple cryo-electron microscopy structures of a plant ABC transporter exporting glutathione derivatives captured a closed conformation proposed to enforce the export directionality, while a complex central to the coupling mechanism containing both glutathione and closed nucleotide binding domains remains elusive.