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Updated: Aug 11, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Crystallization and preliminary X-ray analysis of hyperthermophilic L-threonine dehydrogenase from the archaeon
Noriko Higashi1, Takanori Matsuura, Atsushi Nakagawa
1Research Institute for Cell Engineering, National Institute of Advanced Industrial Science and Technology (AIST Kansai), 1-8-31 Midorigaoka, Ikeda, Osaka 563-8577, Japan.
Abstract:
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. horikoshii L-threonine dehydrogenase crystals belong to space group I4(1)22, with unit-cell parameters a = b = 143.84, c = 304.13 A. The presence of three subunits of the enzyme per asymmetric unit was estimated to give a Matthews coefficient (VM) of 3.5 A3 Da(-1) and a solvent content of 64.7%(v/v).
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