Purification, crystallization and X-ray diffraction analysis of dihydropyrimidinase from Dictyostelium discoideum

Journal Article · Sun Jan 01 04:00:00 EST 2006 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S174430910503976X· OSTI ID:22356238

Lohkamp, Bernhard ^[1]; Andersen, Birgit; Piškur, Jure ^[2]; Dobritzsch, Doreen ^[1]

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1. Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm (Sweden)
2. Department of Cell and Organism Biology, Lund (Sweden)

Dihydropyrimidinase from the slime mould D. discoideum was crystallized. A single crystal was shown to belong to space group I222 and diffracted anisotropically to better than 1.8 Å. Dihydropyrimidinase (EC 3.5.2.2) is the second enzyme in the reductive pyrimidine-degradation pathway and catalyses the hydrolysis of 5,6-dihydrouracil and 5,6-dihydrothymine to the corresponding N-carbamylated β-amino acids. The recombinant enzyme from the slime mould Dictyostelium discoideum was overexpressed, purified and crystallized by the vapour-diffusion method. One crystal diffracted to better than 1.8 Å resolution on a synchrotron source and was shown to belong to space group I222, with unit-cell parameters a = 84.6, b = 89.6, c = 134.9 Å and one molecule in the asymmetric unit.

• OSTI ID: 22356238
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 1 Vol. 62; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
DIFFUSION
MOLECULES
MONOCRYSTALS
RESOLUTION
SPACE GROUPS
X-RAY DIFFRACTION