Open AccessPurification, crystallization and preliminary crystallographic analysis of histone lysine demethylase NO66 from Homo sapiens
Author(s) -
Zhou Xing,
Tao Yue,
Wu Minhao,
Zhang Dandan,
Zang Jianye
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911201740x
Subject(s) - demethylase , histone h3 , crystallography , histone , crystallization , lysine , molecule , chemistry , biochemistry , stereochemistry , amino acid , gene , organic chemistry
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 P 3 1 or P 3 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.