Open AccessCrystallization and preliminary X‐ray diffraction studies of maleylacetate reductase from Rhizobium sp. strain MTP‐10005
Author(s) -
Fujii Tomomi,
Goda Yuko,
Yoshida Masahiro,
Oikawa Tadao,
Hata Yasuo
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108022537
Subject(s) - monoclinic crystal system , ammonium sulfate , crystallization , resorcinol , strain (injury) , reductase , chemistry , crystallography , resolution (logic) , molecule , enzyme , stereochemistry , crystal structure , biochemistry , chromatography , biology , organic chemistry , artificial intelligence , computer science , anatomy
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 C 2, with unit‐cell parameters a = 56.85, b = 121.13, c = 94.09 Å, β = 101.48°, and contained one dimeric molecule in the asymmetric unit. It diffracted to 1.79 Å resolution.