title: 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.
authors.affiliation: Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden.
authors.forename: Stina
authors.initials: S
authors.lastname: Lundgren
authors.forename: Birgit
authors.initials: B
authors.lastname: Andersen
authors.forename: Jure
authors.initials: J
authors.lastname: Piskur
authors.forename: Doreen
authors.initials: D
authors.lastname: Dobritzsch
mesh_terms: D000581:Amidohydrolases / Q000032:analysis* / Q000737:chemistry*; D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D029721:Drosophila Proteins / Q000032:analysis* / Q000737:chemistry*; D004331:Drosophila melanogaster / Q000201:enzymology; D006801:Humans
chemical_list: D029721:Drosophila Proteins; D000581:Amidohydrolases; C021590:beta-ureidopropionase