Crystallization and preliminary crystallographic analysis of  d ‐aspartate oxidase from porcine kidney | Zendy

Senda Miki | Zendy; Yamamoto Atsushi | Zendy; Tanaka Hiroyuki | Zendy; Ishida Tetsuo | Zendy; Horiike Kihachiro | Zendy; Senda Toshiya | Zendy

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Crystallization 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.

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