Sloane D L, Browner M F, Dauter Z, Wilson K, Fletterick R J, Sigal E
Cardiovascular Research Institute (CVRI), University of California, San Francisco 94143.
Biochem Biophys Res Commun. 1990 Dec 14;173(2):507-13. doi: 10.1016/s0006-291x(05)80063-4.
We report a new purification of rabbit reticulocyte 15-lipoxygenase that has resulted in the first crystallization of a mammalian lipoxygenase. The enzyme was purified to homogeneity (greater than 98% pure by SDS-PAGE) using high pressure liquid chromatography on hydrophobic-interaction, hydroxyapatite and cation-exchange columns. Crystals were grown by the vapor diffusion method from concentrated solutions of the protein in sodium phosphate buffer, pH 7.0. The hexagonal, rod-shaped crystals were on average 0.09 mm x 0.09 mm x 0.4 mm, with approximate unit cell dimensions of a = b = 260 A, c = 145 A. The crystals diffract to 5 A resolution.
