Crystallization and preliminary X‐ray diffraction analysis of l‐threonine dehydrogenase (TDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis
The enzyme l‐threonine dehydrogenase catalyses the NAD+‐dependent conversion of l‐threonine to 2‐amino‐3‐ketobutyrate, which is the first reaction of a two‐step biochemical pathway involved in the metabolism of threonine to glycine. Here, the crystallization and preliminary crystallographic analysis of l‐threonine dehydrogenase (Tk‐TDH) from the hyperthermophilic organism Thermococcus kodakaraensis KOD1 is reported. This threonine dehydrogenase consists of 350 amino acids, with a molecular weight of 38 kDa, and was prepared using an Escherichia coli expression system. The purified native protein was crystallized using the hanging‐drop vapour‐diffusion method and crystals grew in the tetragonal space group P43212, with unit‐cell parameters a = b = 124.5, c = 271.1 Å. Diffraction data were collected to 2.6 Å resolution and preliminary analysis indicates that there are four molecules in the asymmetric unit of the crystal.
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