title: Purification, crystallization and preliminary crystallographic analysis of histone lysine demethylase NO66 from Homo sapiens.
abstract: 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 Å. NO66 crystallized in space group P3(1) or P3(2), with unit-cell parameters a = 89.35, b = 89.35, c = 304.86 Å, α = β = 90, γ = 120°, and the crystal is likely to contain four molecules in the asymmetric unit.
authors: Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
authors: Xing
authors: X
authors: Zhou
authors: Yue
authors: Y
authors: Tao
authors: Minhao
authors: M
authors: Wu
authors: Dandan
authors: D
authors: Zhang
authors: Jianye
authors: J
authors: Zang
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D056466:Histone Demethylases / Q000737:chemistry* / Q000302:isolation & purification; D006801:Humans
chemical_list: D056466:Histone Demethylases