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paper

Cryo-EM structures of full-length Tetrahymena ribozyme at 3.1 Å resolution.

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Cryo-EM structures of full-length Tetrahymena ribozyme at 3.1 Å resolution.
["Su Z", "Zhang K", "Kappel K", "Li S", "Palo M", "Pintilie G", "Rangan R", "Luo B", "Wei Y", "Das R"]
Nature PubMed DOI
Abstract

Single-particle cryogenic electron microscopy (cryo-EM) has become a standard technique for determining protein structures at atomic resolution1-3. However, cryo-EM studies of protein-free RNA are in their early days. The Tetrahymena thermophila group I self-splicing intron was the first ribozyme to be discovered and has been a prominent model system for the study of RNA catalysis and structure-function relationships4, but its full structure remains unknown. Here we report cryo-EM structures of ...

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