Ribosomal protein L22 fromThermus thermophilus: sequencing overexpression and crystallisation-Reference-Cited by-同舟云学术

Ribosomal protein L22 fromThermus thermophilus: sequencing overexpression and crystallisation

Published:1995-08-07 Issue:2-3 Volume:369 Page:229-232
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Davydova Natalia L.,Gryaznova Olga I.,Mashchenko Oksana V.,Vysotskaya Valentina S.,Jonsson Bengt-Harald,Al-Karadaghi Salam,Liljas Anders,Garber Maria B.

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(95)00755-X/fullpdf

Reference39 articles.

1. Structure Function and Genetics of Ribosomes;Vasiliev,1986

2. Cooperative and Antagonistic Interactions of Peptidyl-tRNA and Antibiotics with Bacterial Ribosomes

3. Genetic studies of erythromycin resistant mutants of Escherichia coli

4. Protein components of the erythromycin binding site in bacterial ribosomes.

5. Ribosomal protein gene sequence changes in erythromycin-resistant mutants of Escherichia coli

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3. L22 Ribosomal Protein and Effect of Its Mutation on Ribosome Resistance to Erythromycin;Journal of Molecular Biology;2002-09

4. Crystals of a mutant form of ribosomal protein L22 rendering bacterial ribosomes resistant to erythromycin;Acta Crystallographica Section D Biological Crystallography;2001-07-23

5. The crystal structure of ribosomal protein L22 from Thermus thermophilus: insights into the mechanism of erythromycin resistance;Structure;1998-12