Crystallization and preliminary X-ray characterization of D-3-hydroxybutyrate dehydrogenase from Pseudomonas fragi.
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.
Nakajima
Yoshitaka
Y
Biotechnology Department, Graduate School of Biomedical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki 852-8521, Japan.
Ito
Kiyoshi
K
Ichihara
Emi
E
Ogawa
Kyohei
K
Egawa
Takashi
T
Xu
Yue
Y
Yoshimoto
Tadashi
T
D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification; D001483:Base Sequence; D003460:Crystallization; D017931:DNA Primers; D004926:Escherichia coli / Q000201:enzymology; D006884:Hydroxybutyrate Dehydrogenase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D044206:Pseudomonas fragi / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D017356:Synchrotrons; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D017931:DNA Primers; D011994:Recombinant Proteins; D006884:Hydroxybutyrate Dehydrogenase