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Crystallization and preliminary X-ray data analysis of beta-alanine synthase from Drosophila melanogaster.

ABSTRACT: Beta-alanine synthase catalyzes the last step in the reductive degradation pathway for uracil and thymine, which represents the main clearance route for the widely used anticancer drug 5-fluorouracil. Crystals of the recombinant enzyme from Drosophila melanogaster, which is closely related to the human enzyme, were obtained by the hanging-drop vapour-diffusion method. They diffracted to 3.3 A at a synchrotron-radiation source, belong to space group C2 (unit-cell parameters a = 278.9, b = 95.0, c = 199.3 A, beta = 125.8 degrees) and contain 8-10 molecules per asymmetric unit.

SUBMITTER: Lundgren S

PROVIDER: S-EPMC2339735 | biostudies-literature | 2007 Oct

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray data analysis of beta-alanine synthase from Drosophila melanogaster.

Lundgren Stina S Andersen Birgit B Piskur Jure J Dobritzsch Doreen D

Acta crystallographica. Section F, Structural biology and crystallization communications 20070919 Pt 10

Beta-alanine synthase catalyzes the last step in the reductive degradation pathway for uracil and thymine, which represents the main clearance route for the widely used anticancer drug 5-fluorouracil. Crystals of the recombinant enzyme from Drosophila melanogaster, which is closely related to the human enzyme, were obtained by the hanging-drop vapour-diffusion method. They diffracted to 3.3 A at a synchrotron-radiation source, belong to space group C2 (unit-cell parameters a = 278.9, b = 95.0, c ...[more]

PMID: 17909293

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