Obtained a high resolution complex crystal structure of the androgen receptor (AR) and its response element (ARE) could provide a theoretical basis for drug target design for the treatment of prostate cancer. In this study, a prokaryotic expression vector of AR-DBD was constructed, and the protein was inducted to expression at 16 ℃ with 0.5 mmol/L IPTG for 24 h. In order to purify AR-DBD protein easily, the protein purification conditions were optimized by binding to ARE oligo nucleic acids. Finally, we obtained the protein nucleic acid complex crystal that exhibited short rod like three dimensional structures with clear crystal edges. The protein nucleotide complex crystals prepared in this study can be used for X ray diffraction analysis directly.
