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Crystallization and X-ray diffraction data analysis of leukotriene A4 hydrolase from Saccharomyces cerevisiae

Andersson, B; Kull, F; Haeggström, J Z and Thunnissen, Marjolein LU (2003) In Acta Crystallographica. Section D: Biological Crystallography D59(Pt 6). p.1093-1095
Abstract
The Saccharomyces cerevisiae leukotriene A4 (LTA4) hydrolase (scLTA4 hydrolase) has been crystallized in order to study the two activities of LTA4 hydrolase in an evolutionary perspective. Single well diffracting crystals are obtained after switching from the hanging-drop method to liquid-liquid diffusion in capillaries using PEG 8000 as precipitant. These crystals belong to space group P212121, with unit-cell parameters a = 70.8, b = 98.1, c = 99.2 Å. Intensity data to 2.3 Å resolution were collected from a native scLTA4 hydrolase crystal using synchrotron radiation. A molecular-replacement solution was obtained using the human LTA4 hydrolase structure and the program BEAST.
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organization
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type
Contribution to journal
publication status
published
subject
in
Acta Crystallographica. Section D: Biological Crystallography
volume
D59
issue
Pt 6
pages
1093 - 1095
publisher
John Wiley and Sons Inc.
external identifiers
  • pmid:12777785
  • wos:000183043700029
  • scopus:0038044739
ISSN
1399-0047
DOI
10.1107/S0907444903007728
language
English
LU publication?
yes
id
6b52925a-4f36-4cf5-a25f-6d5669e43870 (old id 128466)
date added to LUP
2007-07-09 14:39:16
date last changed
2018-01-07 08:47:49
@article{6b52925a-4f36-4cf5-a25f-6d5669e43870,
  abstract     = {The Saccharomyces cerevisiae leukotriene A4 (LTA4) hydrolase (scLTA4 hydrolase) has been crystallized in order to study the two activities of LTA4 hydrolase in an evolutionary perspective. Single well diffracting crystals are obtained after switching from the hanging-drop method to liquid-liquid diffusion in capillaries using PEG 8000 as precipitant. These crystals belong to space group P212121, with unit-cell parameters a = 70.8, b = 98.1, c = 99.2 Å. Intensity data to 2.3 Å resolution were collected from a native scLTA4 hydrolase crystal using synchrotron radiation. A molecular-replacement solution was obtained using the human LTA4 hydrolase structure and the program BEAST.},
  author       = {Andersson, B and Kull, F and Haeggström, J Z and Thunnissen, Marjolein},
  issn         = {1399-0047},
  language     = {eng},
  number       = {Pt 6},
  pages        = {1093--1095},
  publisher    = {John Wiley and Sons Inc.},
  series       = {Acta Crystallographica. Section D: Biological Crystallography},
  title        = {Crystallization and X-ray diffraction data analysis of leukotriene A4 hydrolase from Saccharomyces cerevisiae},
  url          = {http://dx.doi.org/10.1107/S0907444903007728},
  volume       = {D59},
  year         = {2003},
}