Cryo-electron microscopy has been used to provide a structural interpretation of the complete action cycle of release factor 3 during translation termination, which includes a coordinated sequence of interactions with a class-I release factor and the ribosome.

Structural analysis of translating human mitoribosome illustrates elemental steps of translation in mitochondria.

Nramp-family transporters adapt a common fold to a novel mechanism in which the spatial and temporal separation of like-charge transition metal and proton co-substrates circumvents the expected electrostatic repulsion.

The cryo-EM structures of actomyosin-V, including a novel strongly bound post-rigor transition state, reveal a pronounced structural heterogeneity of myosin-V and the specific selection of the closed D-loop conformation of F-actin.

Crystal structures of an archaeal homologue of mammalian glutamate transporters in apo and ion-only bound outward- and inward-facing states reveal ion-coupled conformational changes supporting mechanisms of coupling, gating, and transport.

Integration of structural bioinformatics and free-energy simulations reveals how a helicase switches its function from unwinding to rezipping DNA, during which a key metastable conformation is predicted and verified by single-molecule measurements.

METTL18 methylates histidine 245 of ribosomal protein RPL3, retards ribosome traversal at tyrosine codons, and thus ensures nascent protein folding for proteostasis maintenance.

The fast spreading of neural activity across the brain has a complex structure, imposed by the white-matter bundles.

Visualization of the real-time conformational transitions of the human voltage-gated proton channel hHv1 provided novel insights into how voltage and pH gradients modify the dynamic behaviors of channel structures to control proton flow across membrane.

An exceedingly low speed limit was estimated for a helical hairpin formation by analyzing hours-long, incessant structural transitions.