Premium
Proteins of the Thermus thermophilus ribosome Purification of several individual proteins and crystallization of protein TL7
Author(s) -
Sedelnikova S.E.,
Agalarov S.C.,
Garber M.B.,
Yusupov M.M.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80910-9
Subject(s) - thermus thermophilus , ribosomal protein , ribosome , escherichia coli , thermophile , chemistry , protein subunit , biochemistry , crystallization , chromatography , sepharose , bacteria , protein purification , ribosomal rna , 50s , biology , enzyme , rna , genetics , organic chemistry , gene
The procedure of selective removal of eight proteins from the 50 S ribosomal subunit of the extreme thermophilic bacterium Thermus thermophilus has been developed based on extraction at 60°C in the presence of 0.5 M or 1 M NH 4 Cl and 50% ethanol. CM‐Sepharose CL column chromatography of the protein mixture under non‐denaturing conditions yielded five proteins with a purity of 95% or higher. Crystals of one of these proteins, namely TL7 (probably an analog of L6 protein from the Escherichia coli ribosome) have been obtained using the ‘hanging drop’ method with ammonium sulphate as a precipitant.