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

ABSTRACT: 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 P2(1), with unit-cell parameters a = 79.38, b = 144.0, c = 80.46 Å, ? = 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.

SUBMITTER: Senda M

PROVIDER: S-EPMC3370900 | biostudies-literature | 2012 Jun

REPOSITORIES: biostudies-literature

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

Senda Miki M Yamamoto Atsushi A Tanaka Hiroyuki H Ishida Tetsuo T Horiike Kihachiro K Senda Toshiya T

Acta crystallographica. Section F, Structural biology and crystallization communications 20120522 Pt 6

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 P2(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. ...[more]

PMID: 22684060

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