Crystallization and preliminary X-ray data analysis of β-alanine synthase from Drosophila melanogaster
- Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm (Sweden)
- Department of Organism and Cell Biology, Lund University, Lund (Sweden)
β-Alanine synthase catalyzes the last step in the reductive degradation pathway for uracil and thymine. Crystals of the recombinant enzyme from D. melanogaster belong to space group C2. Diffraction data to 3.3 Å resolution were collected and analyzed. β-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 Å at a synchrotron-radiation source, belong to space group C2 (unit-cell parameters a = 278.9, b = 95.0, c = 199.3 Å, β = 125.8°) and contain 8–10 molecules per asymmetric unit.
- OSTI ID:
- 22360411
- Journal Information:
- Acta Crystallographica. Section F, Vol. 63, Issue Pt 10; Other Information: PMCID: PMC2339735; PMID: 17909293; PUBLISHER-ID: pu5200; OAI: oai:pubmedcentral.nih.gov:2339735; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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