Crystallization and Preliminary X-Ray Studies of TON_0559, a Putative Member of the Haloacid Dehalogenase (HAD) Superfamily from Thermococcus onnurineus NA1

Authors: Kim, Kyeong K.; Thi Nguyen, Chi My; Lee, Hyun Sook; Cho, Yona; Lee, Jung-Hyun; Ha, Sung Chul; Hwang, Hye-Yeon

Source: Protein and Peptide Letters, Volume 15, Number 2, February 2008 , pp. 235-237(3)

Publisher: Bentham Science Publishers

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Abstract:

To elucidate the molecular basis underlying their broad substrate specificity and reaction mechanism of the enzymes belonging to the haloacid dehalogenase (HAD) superfamily, TON_0559, a putative HAD subfamily protein from a hyperthermophilic archaeon Thermococcus onnurineus NA1, was expressed, purified and crystallized. X-ray diffraction data were collected to 2.0 Å resolution. The space group is C2, with unit cell parameters a = 121.2 Å, b = 62.9 Å, c = 37.5 Å and β= 106.5°.





Keywords: TON_0559; Thermococcus onnurineus; crystallization

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986608783489625

Publication date: February 1, 2008

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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