Open AccessCrystallization and preliminary crystallographic analysis of d ‐aspartate oxidase from porcine kidney
Author(s) -
Senda Miki,
Yamamoto Atsushi,
Tanaka Hiroyuki,
Ishida Tetsuo,
Horiike Kihachiro,
Senda Toshiya
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112013243
Subject(s) - crystallization , molecular replacement , oxidase test , crystallography , peg ratio , chemistry , resolution (logic) , d amino acid oxidase , crystal structure , biochemistry , enzyme , organic chemistry , finance , artificial intelligence , computer science , economics
d ‐Aspartate oxidase (DDO) from porcine kidney was crystallized by the sitting‐drop vapour‐diffusion method using PEG 8000 as a precipitant. The crystal belonged to space group P 2 1 , with unit‐cell parameters a = 79.38, b = 144.0, c = 80.46 Å, β = 101.1°, and diffracted to 1.80 Å resolution. Molecular‐replacement trials using the structure of human d ‐amino‐acid oxidase, which is 42% identical in sequence to DDO, as a search model provided a satisfactory solution.