Crystallization and preliminary X-ray diffraction studies of maleylacetate reductase from Rhizobium sp. strain MTP-10005.
Maleylacetate reductase (EC 1.3.1.32), which catalyzes the reduction of maleylacetate to 3-oxoadipate, plays an important role in the aerobic microbial catabolism of resorcinol. The enzyme has been crystallized at 293 K by the sitting-drop vapour-diffusion method supplemented with a microseeding technique, using ammonium sulfate as the precipitating agent. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a = 56.85, b = 121.13, c = 94.09 A, beta = 101.48 degrees , and contained one dimeric molecule in the asymmetric unit. It diffracted to 1.79 A resolution.
Fujii
Tomomi
T
Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
Goda
Yuko
Y
Yoshida
Masahiro
M
Oikawa
Tadao
T
Hata
Yasuo
Y
D002853:Chromatography, Liquid; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D044925:Oxidoreductases Acting on CH-CH Group Donors / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D012231:Rhizobium / Q000201:enzymology*
D044925:Oxidoreductases Acting on CH-CH Group Donors; C021530:maleylacetate reductase