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

E-ISSN： 1744-3091|67|8|907-910

ISSN： 1744-3091

Source： Acta Crystallographica Section F, Vol.67, Iss.8, 2011-08, pp. : 907-910

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Abstract

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 P4₃, with unit‐cell parameters a = 51.7, b = 51.7, c = 36.2 Å.