Interferon regulatory factor 1 (IRF-1) is an essential factor involved in the regulation of type I interferon (IFN) and IFN-inducible genes. The protein consists of 329 amino acids that are highly conserved from mouse to human. Similar to other transcription factors, the protein is modular in nature with a basic N-terminal region inolved in DNA binding and an acidic C-terminal region required for activation. We report here the expression, purification and co-crystallization of the minimal N-terminal region of IRF-I involved in DNA binding (amino acids 1-113) with a 13 bp DNA fragment from the IFN-β promoter. The crystals diffract to at least 3.0 Å in resolution and belong to space group R3 with unit cell parameters of a = b = 84.8 Å, c = 203.7 Å.
Escalante, C. R., Yie, J., Thanos, D., & Aggarwal, A. K. (1997). Expression, purification, and co-crystallization of IRF-I bound to the interferon-β element PRDI. FEBS Letters, 414(2), 219–220. https://doi.org/10.1016/S0014-5793(97)00996-4