Crystallization of the cpn6O/cpn10 complex (‘holo‐chaperonin’) from Thermus thermophilus

FEBS Letters

Sedelnikova, S.E.¹  Ryazantsev, S.N.¹  Lissin, N.M.¹ 

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

关键词: Molecular chaperone;    Chaperonin;    GroE;    Thermus thermophilus;    Crystallization;    Electron microscopy;    cpn60 and cpn10;    chaperonin 60 and chaperonin 10;    respectively;    TEA;    triethanolamine;    EDTA;    ethylene diamine tetrancetic acid;    DTT;    dithiothreitol;   

DOI  :  10.1016/0014-5793(92)81357-R

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A stable complex of the chaperonins, cpn60 and cpn10 (Escherichia coli GroEL and GroES homologues), from the extremely thermophilic bacterium Thermus thermophilis has been isolated and crystallized. The crystals have dimensions up to 30 × 200 × 200 μm. Ultra-thin sections of the crystals estimated by electron microscopy showed a rectangular lattice with unit cell parameters of a=17 nm, b=27 nm, γ=90°.

【 授权许可】

Unknown