Crystallization and preliminary X-ray analysis of hyperthermophilic L-threonine dehydrogenase from the archaeon Pyrococcus horikoshii.

@article{Higashi2005CrystallizationAP,
  title={Crystallization and preliminary X-ray analysis of hyperthermophilic L-threonine dehydrogenase from the archaeon Pyrococcus horikoshii.},
  author={Noriko Higashi and Takanori Matsuura and Atsushi Nakagawa and Kazuhiko Ishikawa},
  journal={Acta crystallographica. Section F, Structural biology and crystallization communications},
  year={2005},
  volume={61 Pt 4},
  pages={432-4}
}
Recombinant L-threonine dehydrogenase from the hyperthermophilic archaeon Pyrococcus horikoshii was prepared using an Escherichia coli expression system. The hyperthermostable L-threonine dehydrogenase consists of 348 amino acids with a molecular weight of 37.7 kDa. The enzyme was crystallized by the hanging-drop vapour-diffusion method at 277 K and preliminary X-ray crystallographic analysis was carried out. Diffraction data were collected to 2.20 A resolution under cryogenic conditions. P… CONTINUE READING