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

Lohkamp, B; Andersen, Birgit LU ; Piskur, Jure LU and Dobritzsch, D (2006) In Acta Crystallographica. Section F: Structural Biology and Crystallization Communications2005-01-01+01:002014-01-01+01:00 62(1). p.36-38
Abstract
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 beta-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 angstrom 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 angstrom and one molecule in the asymmetric unit.
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Acta Crystallographica. Section F: Structural Biology and Crystallization Communications2005-01-01+01:002014-01-01+01:00
volume
62
issue
1
pages
36 - 38
publisher
Wiley-Blackwell
external identifiers
  • pmid:16511257
  • wos:000234169100011
  • scopus:33646860795
ISSN
2053-230X
DOI
10.1107/s174430910503976x
language
English
LU publication?
yes
id
abddacff-188a-402a-952c-9025759ad191 (old id 421719)
date added to LUP
2007-10-09 09:32:23
date last changed
2019-02-20 07:55:38
@article{abddacff-188a-402a-952c-9025759ad191,
  abstract     = {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 beta-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 angstrom 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 angstrom and one molecule in the asymmetric unit.},
  author       = {Lohkamp, B and Andersen, Birgit and Piskur, Jure and Dobritzsch, D},
  issn         = {2053-230X},
  language     = {eng},
  number       = {1},
  pages        = {36--38},
  publisher    = {Wiley-Blackwell},
  series       = {Acta Crystallographica. Section F: Structural Biology and Crystallization Communications2005-01-01+01:002014-01-01+01:00},
  title        = {Purification, crystallization and X-ray diffraction analysis of dihydropyrimidinase from Dictyostelium discoideum},
  url          = {http://dx.doi.org/10.1107/s174430910503976x},
  volume       = {62},
  year         = {2006},
}