Crystallization and preliminary X-ray analysis of SDR-type pyridoxal dehydrogenase from Mesorhizobium loti.
Pyridoxal 4-dehydrogenase from Mesorhizobium loti MAFF303099 was overexpressed in Escherichia coli. The recombinant selenomethionine-substituted enzyme was purified and crystallized by the sitting-drop vapour-diffusion method using PEG 4000 as precipitant. Crystals grew in the presence of 0.45 mM NAD(+). The crystals diffracted to 2.9 A resolution and belonged to the monoclinic space group P2(1), with unit-cell parameters a = 86.20, b = 51.11, c = 91.73 A, beta = 89.36 degrees. The calculated V(M) values suggested that the asymmetric unit contained four molecules.
Faculty of Agriculture and Agricultural Science Program, Graduate School of Integral Arts and Science, Kochi University, Monobe, Nankoku, Kochi 783-8502, Japan.
Huy Nhat
HN
Chu
Jun
J
Kobayashi
Yu
Y
Yoshikane
Bunzo
B
Mikami
Toshiharu
T
Yagi
D000429:Alcohol Oxidoreductases / Q000737:chemistry*; D020561:Alphaproteobacteria / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray
D000429:Alcohol Oxidoreductases; C042642:pyridoxal dehydrogenase