Ribosomal protein L22 from Thermus thermophilus: sequencing, overexpression and crystallisation

N L Davydova; O I Gryaznova; O V Mashchenko; V S Vysotskaya; B H Jonsson; S al-Karadaghi; A Liljas; M B Garber

doi:10.1016/0014-5793(95)00755-x

Ribosomal protein L22 from Thermus thermophilus: sequencing, overexpression and crystallisation

FEBS Lett. 1995 Aug 7;369(2-3):229-32. doi: 10.1016/0014-5793(95)00755-x.

Authors

N L Davydova¹, O I Gryaznova, O V Mashchenko, V S Vysotskaya, B H Jonsson, S al-Karadaghi, A Liljas, M B Garber

Affiliation

¹ Molecular Biophysics, University of Lund, Sweden.

PMID: 7649262
DOI: 10.1016/0014-5793(95)00755-x

Abstract

The gene for the ribosomal protein L22 from Thermus thermophilus has been sequenced and overexpressed in Escherichia coli. A multiple sequence alignment was carried out for all proteins of the L22 family reported so far. The recombinant protein was purified and crystallized. The crystals belong to the space group P2(1)2(1)2(1), with cell parameters of a = 32.6 A, b = 66.0 A, c = 67.8 A.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Base Sequence
Cloning, Molecular
Crystallization
Crystallography, X-Ray
Escherichia coli / genetics
Escherichia coli Proteins*
Genes, Bacterial / genetics*
Molecular Sequence Data
RNA-Binding Proteins / biosynthesis
RNA-Binding Proteins / chemistry
RNA-Binding Proteins / genetics*
RNA-Binding Proteins / isolation & purification
Recombinant Proteins / biosynthesis
Recombinant Proteins / isolation & purification
Ribosomal Proteins*
Sequence Alignment
Sequence Analysis, DNA
Thermus thermophilus / genetics*

Substances

Escherichia coli Proteins
RNA-Binding Proteins
Recombinant Proteins
Ribosomal Proteins
rplV protein, E coli

Associated data

GENBANK/X84708