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Journal article

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

Abstract:
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 A, and diffract to 2.4 A using Cu Kalpha radiation.
Publication status:
Published

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Publisher copy:
10.1107/s0907444900019818

Authors


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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
Journal:
Acta crystallographica. Section D, Biological crystallography
Volume:
57
Issue:
Pt 3
Pages:
425-427
Publication date:
2001-03-01
DOI:
EISSN:
1399-0047
ISSN:
0907-4449
Source identifiers:
31824
Language:
English
Keywords:
Pubs id:
pubs:31824
UUID:
uuid:cb7201e9-65bb-4c4a-ab08-56496200929a
Local pid:
pubs:31824
Deposit date:
2012-12-19

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