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

Lundgren, Stina ; Andersen, Birgit LU ; Piskur, Jure LU and Dobritzsch, Doreen (2007) In Acta Crystallographica. Section F: Structural Biology and Crystallization Communications 63. p.874-877
Abstract
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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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Acta Crystallographica. Section F: Structural Biology and Crystallization Communications
volume
63
pages
874 - 877
publisher
Wiley-Blackwell
external identifiers
  • wos:000250012400014
  • scopus:34848926196
  • pmid:17909293
ISSN
2053-230X
DOI
10.1107/S1744309107042984
language
English
LU publication?
yes
id
2d052e19-92d7-4243-86ea-c0f75e3f0906 (old id 655559)
date added to LUP
2016-04-01 17:11:20
date last changed
2022-01-29 01:00:53
@article{2d052e19-92d7-4243-86ea-c0f75e3f0906,
  abstract     = {{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.}},
  author       = {{Lundgren, Stina and Andersen, Birgit and Piskur, Jure and Dobritzsch, Doreen}},
  issn         = {{2053-230X}},
  language     = {{eng}},
  pages        = {{874--877}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{Acta Crystallographica. Section F: Structural Biology and Crystallization Communications}},
  title        = {{Crystallization and preliminary X-ray data analysis of beta-alanine synthase from Drosophila melanogaster}},
  url          = {{http://dx.doi.org/10.1107/S1744309107042984}},
  doi          = {{10.1107/S1744309107042984}},
  volume       = {{63}},
  year         = {{2007}},
}