Cryo-EM structures of 70S•RelA ribosome complexes reveal how cognate deacyl-tRNA activates RelA.

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.

Ensemble cryo-EM visualizes how structural rearrangements poise the newly made protein and release factor RF2 to dissociate in preparation for ribosome recycling.

Nascent regulatory peptides tune the translation rate through a continuous, dynamic reshaping of the functional center of the ribosome.

An enrichable cross-linker with optional isotope labeling quadruples the number of cross-linked peptides identified from high-complexity samples, enhancing proteome-wide analysis of protein-protein interactions and protein conformational changes by mass spectrometry.

By sterically hindering tRNA binding and inhibiting translation elongation, mRNA stem-loops can modulate gene expression.

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.

Cryo-EM structures of the 30S*RNAP complex visualize co-localization of the transcription and translation machineries and provide insights into the transcription-translation synchrony, which coordinates gene expression in bacteria.

The interaction of SecA with its substrate proteins is regulated by its evolutionarily conserved C-terminal tail, which autoinhibits SecA unless SecA binds to the ribosome.

Proteins can fold deeper inside ribosomes with an enlarged exit tunnel.