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Purification, crystallization and preliminary X-ray diffraction of anthocyanidin synthase from Arabidopsis thaliana
J J Turnbull1, A G Prescott, C J Schofield
1The Dyson Perrins Laboratory and Oxford Centre for Molecular Sciences, South Parks Road, Oxford OX1 3QY, England.
Acta Crystallographica. Section D, Biological Crystallography
|February 27, 2001
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.