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

Abstract

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.

Authors:
 [1]; ;  [2];  [1]
  1. Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm (Sweden)
  2. Department of Cell and Organism Biology, Lund (Sweden)
Publication Date:
OSTI Identifier:
22356238
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 62; Journal Issue: Pt 1; Other Information: PMCID: PMC2150923; PMID: 16511257; PUBLISHER-ID: en5141; OAI: oai:pubmedcentral.nih.gov:2150923; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; DIFFUSION; MOLECULES; MONOCRYSTALS; RESOLUTION; SPACE GROUPS; X-RAY DIFFRACTION

Citation Formats

Lohkamp, Bernhard, Andersen, Birgit, Piškur, Jure, and Dobritzsch, Doreen, E-mail: doreen.dobritzsch@ki.se. Purification, crystallization and X-ray diffraction analysis of dihydropyrimidinase from Dictyostelium discoideum. United Kingdom: N. p., 2006. Web. doi:10.1107/S174430910503976X.
Lohkamp, Bernhard, Andersen, Birgit, Piškur, Jure, & Dobritzsch, Doreen, E-mail: doreen.dobritzsch@ki.se. Purification, crystallization and X-ray diffraction analysis of dihydropyrimidinase from Dictyostelium discoideum. United Kingdom. doi:10.1107/S174430910503976X.
Lohkamp, Bernhard, Andersen, Birgit, Piškur, Jure, and Dobritzsch, Doreen, E-mail: doreen.dobritzsch@ki.se. Sun . "Purification, crystallization and X-ray diffraction analysis of dihydropyrimidinase from Dictyostelium discoideum". United Kingdom. doi:10.1107/S174430910503976X.
@article{osti_22356238,
title = {Purification, crystallization and X-ray diffraction analysis of dihydropyrimidinase from Dictyostelium discoideum},
author = {Lohkamp, Bernhard and Andersen, Birgit and Piškur, Jure and Dobritzsch, Doreen, E-mail: doreen.dobritzsch@ki.se},
abstractNote = {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.},
doi = {10.1107/S174430910503976X},
journal = {Acta Crystallographica. Section F},
number = Pt 1,
volume = 62,
place = {United Kingdom},
year = {Sun Jan 01 00:00:00 EST 2006},
month = {Sun Jan 01 00:00:00 EST 2006}
}