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

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 54; no. 6-2; pp. 1419 - 1421
• Main Authors: Bell, Graeme S., Russell, Rupert J. M., Kohlhoff, Michael, Hensel, Reinhard, Danson, Michael J., Hough, David W., Taylor, Garry L.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.11.1998
• Subjects: Bacterial Proteins - chemistry; Bacterial Proteins - isolation & purification; Biopolymers; Cloning, Molecular; Crystallization; Crystallography, X-Ray; Escherichia coli; Protein Conformation; Pyrococcus - enzymology; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - isolation & purification; Triose-Phosphate Isomerase - chemistry; Triose-Phosphate Isomerase - isolation & purification
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444998004910

Recombinant triosephosphate isomerase (TIM) from a hyperthermophilic Archaeon, Pyrococcus woesei, has been crystallized. Three crystal forms have been obtained: monoclinic, orthorhombic and hexagonal. The monoclinic crystals belong to space group P21 with cell dimensions a = 79.1, b = 89.2, c = 145.4 Å and β = 92.8°, and diffract to at least 2.6 Å. The orthorhombic crystals belong to space group P21212 with a = 89.4, b = 155.9, c = 79.5 Å, and diffract to 2.9 Å. Diffraction from the hexagonal form showed extensive disorder. The monoclinic form contains two tetramers in the asymmetric unit, which are in the same orientation but related by a pseudo‐centring. The orthorhombic form contains one tetramer in the asymmetric unit which is in approximately the same orientation as in the monoclinic form. Knowledge of the structure of this hyperthermostable TIM, which is tetrameric in contrast to dimeric forms previously observed, will add to the understanding of protein thermostability.