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


Noriko Higashia, Takanori Matsuurab, Atsushi Nakagawab and Kazuhiko Ishikawaa*

aResearch Institute for Cell Engineering, National Institute of Advanced Industrial Science and Technology (AIST Kansai), 1-8-31 Midorigaoka, Ikeda, Osaka 563-8577, Japan,
bInstitute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan

Acta Crystallographica F61(4), 432-434 (2005)

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 Å resolution under cryogenic conditions. P. horikoshii L-threonine dehydrogenase crystals belong to space group I4122, with unit-cell parameters a = b = 143.84, c = 304.13 Å. The presence of three subunits of the enzyme per asymmetric unit was estimsted to give a Matthews coefficient (VM) of 3.5 Å3 Da-1 and a solvent content of 64.7%(v/v).




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