Crystallization and preliminary crystallographic analysis of d-aspartate oxidase from porcine kidney

被引：2
|
作者：
Senda, Miki [2 ]
Yamamoto, Atsushi [3 ]
Tanaka, Hiroyuki [3 ]
Ishida, Tetsuo [3 ]
Horiike, Kihachiro [3 ]
Senda, Toshiya [1 ]
机构：
[1] Natl Inst Adv Ind Sci & Technol, BIRC, Koto Ku, Tokyo 1350064, Japan
[2] Japan Biol Informat Consortium JBIC, JBIC Res Inst, Struct Guided Drug Dev Project, Koto Ku, Tokyo 1350064, Japan
[3] Shiga Univ Med Sci, Dept Biochem & Mol Biol, Otsu, Shiga 5202192, Japan
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2012年 / 68卷
关键词：
d-aspartate oxidase; FAD; flavoproteins; anaerobic crystallization; AMINO-ACID OXIDASE; CRYSTAL-STRUCTURE; MECHANISM; PROTEIN;
D O I：
10.1107/S1744309112013243
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
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 P21, with unit-cell parameters a = 79.38, b = 144.0, c = 80.46 angstrom, beta = 101.1 degrees, and diffracted to 1.80 angstrom 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.
引用
收藏
页码：644 / 646
页数：3
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