Proteins of the Thermus thermophilus ribosome Purification of several individual proteins and crystallization of protein TL7

FEBS Letters

Agalarov, S.C.¹  Garber, M.B.¹  Yusupov, M.M.¹  Sedelnikova, S.E.¹ 

[1] Institute of Protein Research, Academy of Sciences of the USSR, 142292 Pushchino, Moscow Region, USSR

关键词: Ribosomal protein;    Crystallization;    Purification;    (Thermus thermophilus);   

DOI  :  10.1016/0014-5793(87)80910-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 NH₄Cl 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.

【 授权许可】

Unknown