Crystallization of the chaperonin GroEL-GroES complex from Thermus thermophilus HB8.
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 A, alpha = 82.9, beta = 85.4, gamma = 68.5 degrees. The crystal asymmetric unit contains two molecules (MW = 885 kDa). One data set to 3.0 A 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.
Shimamura
Tatsuro
T
Department of Biological Sciences, Imperial College, London SW7 2AZ, England.
Koike-Takeshita
Ayumi
A
Yokoyama
Ken
K
Yoshida
Masasuke
M
Taguchi
Hideki
H
Iwata
So
S
D018835:Chaperonin 10 / Q000737:chemistry*; D018834:Chaperonin 60 / Q000737:chemistry*; D003460:Crystallization; D011485:Protein Binding; D011487:Protein Conformation; D016963:Thermus thermophilus / Q000737:chemistry*; D014961:X-Ray Diffraction
D018835:Chaperonin 10; D018834:Chaperonin 60