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

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

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8405103

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

About this item

Full title

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

Publisher

London: Nature Publishing Group UK

Journal title

Nature (London), 2021-08, Vol.596 (7873), p.603-607

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Single-particle cryogenic electron microscopy (cryo-EM) has become a standard technique for determining protein structures at atomic resolution
1

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...

Alternative Titles

Full title

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

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8405103

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8405103

Other Identifiers

ISSN

0028-0836,1476-4687

E-ISSN

1476-4687

DOI

10.1038/s41586-021-03803-w

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