Preliminary crystallographic studies of triosephosphate isomerase (TIM) from the hyperthermophilic Archaeon Pyrococcus woesei

Recombinant triosephosphate isomerase (TIM) from a hyperthermophilic Archae on, Pyrococcus woesei, has been crystallized. Three crystal forms have been obtained: monoclinic, orthorhombic and hexagonal. The monoclinic crystals belong to space group P2(1) with cell dimensions a = 79.1, b = 89.2, c = 14 5.4 Angstrom and beta = 92.8 degrees, and diffract to at least 2.6 Angstrom . The orthorhombic crystals belong to space group P2(1)2(1)2 with a = 89.4, b = 155.9, c = 79.5 Angstrom, and diffract to 2.9 Angstrom. Diffraction fr om the hexagonal form showed extensive disorder. The monoclinic form contai ns two tetramers in the asymmetric unit, which are in the same orientation but related by a pseudo-centring. The orthorhombic form contains one tetram er in the asymmetric unit which is in approximately the same orientation as in the monoclinic form. Knowledge of the structure of this hyperthermostab le TIM, which is tetrameric in contrast to dimeric forms previously observe d, will add to the understanding of protein thermostability.