Crystallization and X-ray diffraction data analysis of leukotriene A4 hydrolase from Saccharomyces cerevisiae.
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 P2(1)2(1)2(1), with unit-cell parameters a = 70.8, b = 98.1, c = 99.2 A. Intensity data to 2.3 A 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.
Andersson
Björn
B
Department of Biochemistry and Biophysics, Stockholm University, S-106 91 Stockholm, Sweden.
Kull
Filippa
F
Haeggström
Jesper Z
JZ
Thunnissen
Marjolein M G M
MM
D003460:Crystallization; D018360:Crystallography, X-Ray; D018076:DNA, Complementary / Q000096:biosynthesis / Q000235:genetics; D004851:Epoxide Hydrolases / Q000737:chemistry* / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D014961:X-Ray Diffraction
D018076:DNA, Complementary; D004851:Epoxide Hydrolases; C043134:leukotriene A4 hydrolase