Crystallization and preliminary crystallographic analysis of deoxyuridine 5'-triphosphate nucleotidohydrolase from Bacillus subtilis.

Journal article

Single crystals of purified homotrimeric deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) from Bacillus subtilis have been grown under several different conditions using vapour diffusion. X-ray diffraction data have been collected using synchrotron radiation from three crystal forms of the unliganded enzyme and from enzyme cocrystallized with a substrate analogue and inhibitor, dUDP, and a metal ion, Sr(2+). The three crystal forms of unliganded enzyme belong to hexagonal (P6(3)), orthorhombic (P2(1)2(1)2) and cubic (P2(1)3) space groups and data have been recorded to 1.75, 1.90 and 2.50 A spacing, respectively. Crystals grown in the presence of dUDP and Sr(2+) belong to the orthorhombic space group P2(1)2(1)2(1) and data were measured to 1.90 A spacing. Solution of the hexagonal crystal form by molecular replacement using the dUTPase from feline immunodeficiency virus as a search model is in progress.

Authors: Persson, R; Harkiolaki, M; McGeehan, J; Wilson, K

• Publication status: Published
• Journal: Acta crystallographica. Section D, Biological crystallography
• Volume: 57
• Issue: Pt 6
• Pages: 876-878
• Publication date: 2001-06-01
• DOI: 10.1107/s0907444901007727
• EISSN: 1399-0047
• ISSN: 0907-4449
• Language: English
• Keywords: Crystallization; Pyrophosphatases; Protein Conformation; Bacillus subtilis; Crystallography, X-Ray