| Literature DB >> 29903714 |
Amy Jobe1, Zheng Liu1, Cristina Gutierrez-Vargas2, Joachim Frank1,2.
Abstract
In the past 4 years, because of the advent of new cameras, many ribosome structures have been solved by cryoelectron microscopy (cryo-EM) at high, often near-atomic resolution, bringing new mechanistic insights into the processes of translation initiation, peptide elongation, termination, and recycling. Thus, cryo-EM has joined X-ray crystallography as a powerful technique in structural studies of translation. The significance of this new development is that structures of ribosomes in complex with their functional binding partners can now be determined to high resolution in multiple states as they perform their work. The aim of this article is to provide an overview of these new studies and assess the contributions they have made toward an understanding of translation and translational control.Mesh:
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Year: 2019 PMID: 29903714 PMCID: PMC6314068 DOI: 10.1101/cshperspect.a032615
Source DB: PubMed Journal: Cold Spring Harb Perspect Biol ISSN: 1943-0264 Impact factor: 10.005