Skip to main content
padlock icon - secure page this page is secure

Crystallization and preliminary X‐ray diffraction analysis of l‐threonine dehydrogenase (TDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis

Buy Article:

$52.00 + tax (Refund Policy)

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.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: l‐threonine dehydrogenase; thermophiles

Document Type: Research Article

Publication date: September 1, 2008

  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
X
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more