Acta Crystallographica Section D

Biological Crystallography

Volume 59, Part 6 (June 2003)

crystallization papers

Acta Cryst. (2003). D59, 1093-1095 [ doi:10.1107/S0907444903007728 ]

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

B. Andersson, F. Kull, J. Z. Haeggström and M. M. G. M. Thunnissen

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.

Keywords: leukotriene A₄ hydrolase; aminopeptidases.