2003•Acta Crystallographica Section D Biological CrystallographyRequires access

Crystallization of the chaperonin GroEL–GroES complex fromThermus thermophilusHB8

Tatsuro Shimamura, Ayumi Koike‐Takeshita, Ken Yokoyama, Masasuke Yoshida, Hideki Taguchi, So Iwata

Abstract

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.

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Key concepts: GroEL, Thermus thermophilus, GroES, Chaperonin, Crystallography, Thermophile, Escherichia coli, Thermus