Purification, crystallization and preliminary X-ray diffraction of anthocyanidin synthase from Arabidopsis thaliana.
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.
The Dyson Perrins Laboratory and Oxford Centre for Molecular Sciences, South Parks Road, Oxford OX1 3QY, England.
J J
JJ
Turnbull
A G
AG
Prescott
C J
CJ
Schofield
R C
RC
Wilmouth
D017360:Arabidopsis / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D010105:Oxygenases / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation
D010105:Oxygenases; C118159:anthocyanidin synthase