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.

Rapidly proliferating cells are at risk of compromised cell fitness due to proteostasis collapse from perturbations that interfere with ribosome biogenesis.

Ribosomal proteins Rps27 (eS27) and Rps27l (eS27L) are an ancient pair of duplicated genes that encode functionally interchangeable proteins, yet have been evolutionarily retained because both copies are necessary to achieve protein expression across cell types.

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.

BUD23 links ribosome function with mitochondrial protein expression and efficient oxidative phosphorylation by promoting selective mRNA translation and is therefore critical to mouse development and postnatal cardiac function.

Comprehensive structural and compositional characterization of the in vivo 30S ribosomal assembly landscape reveals parallel pathways for 3′-domain formation and a previously unknown role for the assembly factor RimP.

The size of the mRNA fragment protected by a ribosome depends on the ribosome's conformation, which enables studies of the distinct steps of decoding and translocation at single-codon resolution.

Endothelial Differentiation Factor 1 (EDF1) plays a critical role in driving mRNA-specific quality control and global transcriptional responses in response to ribosome collisions.

Mining electron cryomicroscopy data reveals new ribosomal interactions that preclude translation to potentially regulate gene expression.

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