ENGINEERING OF DIFFRACTION-QUALITY CRYSTALS OF THE NF-KAPPA-B P52 HOMODIMER-DNA COMPLEX

The eukaryotic transcription factors NF-kappa B P50 and NF-kappa B P52 are closely related members of the Rel family. Growth of diffraction- quality NF-kappa-B P52:DNA co-crystals crucially depended on (a) exten sive screens for the DNA fragment of optimal length and (b) engineerin g of the protein based on the two known NF-kappa B P50:DNA co-crystal structures [Muller et al. (1995) Nature 373, 311-317; Ghosh et al. (19 95) Nature 373, 303-310]; namely, deletion of 12 C-terminal amino acid residues. These residues are part of the Rel homology region and comp rise the nuclear localization signal. The approach might be of general use for the crystallization of other Rel protein: DNA complexes and i n our case yielded co-crystals which diffract beyond 2.0 Angstrom reso lution. (C) 1997 Federation of European Biochemical Societies.