Crystallization and preliminary crystallographic analysis of a PHD domain of human JARID1B

Xue Guo, Youwei Xu, Ping Wang, Ze Li, Yanhui Xu, Huirong Yang
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications 2011 August 1, 67 (Pt 8): 907-10
Histone lysine methylation can be removed by proteins containing JmjC domains in a sequence- and methylation state-specific manner. JARID1B, a protein containing PHD and JmjC domains, is a histone demethylase specific for H3K4me2 and H3K4me3 which requires Fe(II) and α-ketoglutarate (α-KG) as cofactors to remove the methyl group. JARID1B has also been shown to play a critical role in the development of breast cancer. JARID1B contains JmjN, Arid and JmjC domains, a C5HC2 zinc-finger domain and three PHD domains. The first PHD domain (PHD1(JARID1B); residues 306-360) is located at the N-terminus and is important for both histone demethylase activity and histone-tail recognition of JARID1B. Here, the expression, purification and crystallization of PHD1(JARID1B) is reported. A PHD1(JARID1B) crystal was grown by the hanging-drop vapour-diffusion method in reservoir solution consisting of 0.1 M HEPES pH 7.0, 2.2 M ammonium sulfate at 277 K. A zinc SAD data set was collected from a PHD1(JARID1B) crystal. The diffraction pattern of the PHD1(JARID1B) crystal extended to 1.65 Å resolution using synchrotron radiation. The crystal belonged to space group P4(3), with unit-cell parameters a = 51.7, b = 51.7, c = 36.2 Å.

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