Structure of the human 80S ribosome

Ribosomes are translational machineries that catalyse protein synthesis. Ribosome structures from various species are known at the atomic level, but obtaining the structure of the human ribosome has remained a challenge; efforts to address this would be highly relevant with regard to human diseases. Here we report the near-atomic structure of the human ribosome derived from high-resolution single-particle cryo-electron microscopy and atomic model building. The structure has an average resolution of 3.6 A, reaching 2.9 A resolution in the most stable regions. It provides unprecedented insights into ribosomal RNA entities and amino acid side chains, notably of the transfer RNA binding sites and specific molecular interactions with the exit site tRNA. It reveals atomic details of the subunit interface, which is seen to remodel strongly upon rotational movements of the ribosomal subunits. Furthermore, the structure paves the way for analysing antibiotic side effects and diseases associated with deregulated protein synthesis. The structure of the human ribosome at high resolution has been solved; by combining single-particle cryo-EM and atomic model building, local resolution of 2.9 A was achieved within the most stable areas of the structure. This paper presents the near-atomic structure of the human ribosome determined using single-particle cryo-electron microscopy and atomic model building. The structure reaches the high resolution of 2.9 A in the most stable regions of the complex, allowing the visualization of previously inaccessible elements, such as regions of the ribosomal RNA scaffolding and amino acid side chains. In addition, the significant remodelling of the interface between the large and small subunits is clarified.