Purification, crystallization and preliminary crystallographic analysis of histone lysine demethylase NO66 from Homo sapiens

NO66 is a JmjC domain-containing histone demethylase with specificity towards histone H3 methylated on both Lys4 and Lys36 in vitro and in vivo. A fragment of NO66 lacking the N-terminal 167 amino-acid residues was overexpressed in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion method. X-ray diffraction data were collected to a resolution of 2.29 angstrom. NO66 crystallized in space group P3(1) or P3(2), with unit-cell parameters a = 89.35, b = 89.35, c = 304.86 angstrom, alpha = beta = 90, gamma = 120 degrees, and the crystal is likely to contain four molecules in the asymmetric unit.