Crystallization and X-ray diffraction data analysis of leukotriene A4 hydrolase from Saccharomyces cerevisiae
(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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/128466
- author
- Andersson, B ; Kull, F ; Haeggström, J Z and Thunnissen, Marjolein LU
- organization
- publishing date
- 2003
- 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 & 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
- 2016-04-01 15:47:38
- date last changed
- 2022-04-22 17:27:41
@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 & 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}}, doi = {{10.1107/S0907444903007728}}, volume = {{D59}}, year = {{2003}}, }