Determination of the ribosome structure to a resolution of 2.5 Å by single‐particle cryo‐EM
Year: 2016
Type: review
Abstract: With the advance of new instruments and algorithms, and the accumulation of experience over decades, single‐particle cryo‐EM has become a pivotal part of structural biology. Recently, we determined the structure of a eukaryotic ribosome at 2.5 Å for the large subunit. The ribosome was derived from Trypanosoma cruzi, the protozoan pathogen of Chagas disease. The high‐resolution density map allowed us to discern a large number of unprecedented details including rRNA modifications, water molecules, and ions such as Mg2+ and Zn2+. In this paper, we focus on the procedures for data collection, image processing, and modeling, with particular emphasis on factors that contributed to the attainment of high resolution. The methods described here are readily applicable to other macromolecules for high‐resolution reconstruction by single‐particle cryo‐EM.
Source: Protein Science
DOI: 10.1002/pro.3068
Language: English
Subfield: Structural Biology
Domain: Life Sciences
Open Access status: bronze
Awards: G3030999216, Structural Analysis of Macromolecular Assemblies, G3331595142, Time-resolved Cryo-EM of Short-lived States in Eukaryotic Translation, G5462070209, Graduate Research Fellowship Program (GRFP), G9000014357, Structural and functional studies of mRNA processing, stability and quality control
OpenAlex ID: W2536051193