Abstract: Objective Purification and crystallization of human PHF8. Methods The plasmid PHF8/pet28b, constructed by molecular cloning, was transformed into Rosetta2 (DE3) cell, and PHF8 was induced by IPTG. Recombinant protein was purified, crystallized, and diffracted and its structure was solved. Result Recombinant PHF8 protein was expressed in E. coli, and subjected to affinity purification followed by gel filtration separation. PHF8 protein with hexagon-1ike crystals was obtained. Conclusion The enzymatically active PHF8 protein was purified using the prokaryotic expression system, its crystal particle was obtained, and the overall structure of PHF8 catalytic core was resolved.