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

页码：644 / 646

页数：3

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