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

被引：5
作者：
Lundgren, Stina
Andersen, Birgit
Piskur, Jure
Dobritzsch, Doreen [1 ]
机构：
[1] Karolinska Inst, Dept Med Biochem & Biophys, Stockholm, Sweden
[2] Lund Univ, Dept Organism & Cell Biol, Lund, Sweden
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2007年 / 63卷
关键词：
D O I：
10.1107/S1744309107042984
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
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 angstrom at a synchrotron-radiation source, belong to space group C2 (unit-cell parameters a = 278.9, b = 95.0, c = 199.3 angstrom, beta = 125.8 degrees) and contain 8-10 molecules per asymmetric unit.
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页码：874 / 877
页数：4
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