High-resolution crystal structure of the isolated ribosomal L1 stalk-Reference-Cited by-同舟云学术

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High-resolution crystal structure of the isolated ribosomal L1 stalk

Published:2012-07-17 Issue:8 Volume:68 Page:1051-1057
ISSN:0907-4449
Container-title:Acta Crystallographica Section D Biological Crystallography
language:
Short-container-title:Acta Crystallogr D Biol Cryst

Author:

Tishchenko S.,Gabdulkhakov A.,Nevskaya N.,Sarskikh A.,Kostareva O.,Nikonova E.,Sycheva A.,Moshkovskii S.,Garber M.,Nikonov S.

Publisher

International Union of Crystallography (IUCr)

Subject

General Medicine,Structural Biology

Link

http://journals.iucr.org/d/issues/2012/08/00/mh5065/mh5065.pdf

Reference27 articles.

1. PHENIX: building new software for automated crystallographic structure determination

2. Visualization of the Hybrid State of tRNA Binding Promoted by Spontaneous Ratcheting of the Ribosome

3. Principles of protein–protein recognition

4. Following movement of the L1 stalk between three functional states in single ribosomes

5. Magnesium ions mediate contacts between phosphoryl oxygens at positions 2122 and 2176 of the 23S rRNA and ribosomal protein L1

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2. Features of smaller ribosomes in candidate phyla radiation (CPR) bacteria revealed with a molecular evolutionary analysis;RNA;2022-06-10

3. Structural basis for PoxtA-mediated resistance to phenicol and oxazolidinone antibiotics;Nature Communications;2022-04-06

4. Annealing synchronizes the 70 S ribosome into a minimum-energy conformation;Proceedings of the National Academy of Sciences;2022-02-17

5. Structural Investigations of RNA–Protein Complexes in Post-Ribosomal Era;Crystallography Reports;2021-09

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