MilliporeSigma
  • Crystallization and preliminary X-ray characterization of D-3-hydroxybutyrate dehydrogenase from Pseudomonas fragi.

Crystallization and preliminary X-ray characterization of D-3-hydroxybutyrate dehydrogenase from Pseudomonas fragi.

Acta crystallographica. Section F, Structural biology and crystallization communications (2006-03-02)
Yoshitaka Nakajima, Kiyoshi Ito, Emi Ichihara, Kyohei Ogawa, Takashi Egawa, Yue Xu, Tadashi Yoshimoto
ABSTRACT

A recombinant form of D-3-hydroxybutyrate dehydrogenase (EC 1.1.1.30) from Pseudomonas fragi has been crystallized by the hanging-drop method using PEG 3000 as a precipitating agent. The crystals belong to the orthorhombic group P2(1)2(1)2, with unit-cell parameters a = 64.3, b = 99.0, c = 110.2 A. The crystals are most likely to contain two tetrameric subunits in the asymmetric unit, with a VM value of 3.29 A3 Da(-1). Diffraction data were collected to a 2.0 A resolution using synchrotron radiation at the BL6A station of the Photon Factory.

MATERIALS
Product Number
Brand
Product Description

Roche
3-Hydroxybutyrate Dehydrogenase (3-HBDH), suspension, ~3 units/mg protein (At 25 °C with 3-hydroxybutyrate as the substrate; standardized with BSA.), grade II