Crystallization of the chaperonin GroEL-GroES complex from Thermus thermophilus HB8

被引：6
|
作者：
Shimamura, T
Koike-Takeshita, A
Yokoyama, K
Yoshida, M
Taguchi, H
Iwata, S [1 ]
机构：
[1] Univ London Imperial Coll Sci Technol & Med, Dept Biol Sci, London SW7 2AZ, England
[2] Tokyo Inst Technol, Chem Resources Lab, Kanagawa 2268503, Japan
[3] Japan Sci & Technol Corp, ATP Syst Project, Exploratory Res Adv Technol, Kanagawa 2260026, Japan
[4] Japan Sci & Technol Corp, Precursory Res Embryon Sci & Technol, Kanagawa 2260026, Japan
[5] Univ London Imperial Coll Sci Technol & Med, Div Biomed Sci, London SW7 2AZ, England
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2003年 / 59卷
关键词：
D O I：
10.1107/S0907444903013660
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
The chaperonin GroEL-GroES (GroEL/ES) complex from a thermophilic eubacteria, Thermus thermophilus HB8, has been purified and crystallized. The GroEL/ES complex is known to be composed of 14 identical GroEL subunits (58 kDa) and seven identical GroES subunits (11 kDa). The GroEL/ES complex crystals belong to the triclinic space group P1, with unit-cell parameters a=140.4, b=156.4, c =273.1 Angstrom, alpha=82.9, beta=85.4, gamma=68.5degrees. The crystal asymmetric unit contains two molecules (MW=885 kDa). One data set to 3.0 Angstrom resolution, with 383 652 independent observations (89.3% complete) and an R-merge of 0.08, has been collected from a single crystal. A molecular-replacement solution was obtained using the structure of the GroEL/ES complex from Escherichia coli as a search model.
引用
收藏
页码：1632 / 1634
页数：3
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