Purification, crystallization and preliminary X-ray diffraction of anthocyanidin synthase from Arabidopsis thaliana

被引：17

作者：

Turnbull, JJ

Prescott, AG

Schofield, CJ

Wilmouth, RC

机构：

[1] Dyson Perrins Lab, Oxford OX1 3QY, England

[2] Oxford Ctr Mol Sci, Oxford OX1 3QY, England

[3] John Innes Ctr Plant Sci Res, Dept Appl Genet, Norwich NR4 7UH, Norfolk, England

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2001年 / 57卷

关键词：

D O I：

10.1107/S0907444900019818

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Anthocyanidin synthase (ANS) from Arabidopsis thaliana is a non-haem iron(II)-dependent dioxygenase reported to catalyse the conversion of leucoanthocyanidins to anthocyanidins. Anthocyanidins are precursors of anthocyanins, which are a major family of pigments in higher plants. ANS was crystallized by the vapour-diffusion method using polyethylene glycol as a precipitant. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 61.0, b = 73.2, c = 87.0 Angstrom, and diffract to 2.4 Angstrom using Cu K alpha radiation.

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收藏

页码：425 / 427

页数：3

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