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. 2004 Dec 17;6(1):39–45. doi: 10.1038/sj.embor.7400314

Figure 1.

Figure 1

Protein and DNA constructs used in the crystallization of the TRF1-Dbd and TRF2-Dbd complexes. (A) Schematic representation of the TRF1 and TRF2 proteins indicating the location of the two domains of sequence homology: the TRFH dimerization domain (yellow) and the Myb DNA-binding motif (red). The percentage sequence identity and homology are shown. (B) TRF1 and TRF2 protein constructs used in crystallization. The sequences of the two Dbds have been aligned, and identical (marked with an asterisk) and similar (marked with a dot) residues between TRF1 and TRF2 are denoted. The open rectangles indicate the position of the α-helices. In each case, the N-terminus of the protein is disordered, and the first residue for which there is electron density is residue R380 in TRF1 and K447 in TRF2. (C) The two DNA binding sites used in the crystals. The two sets of three G-C base pairs present in each binding site are highlighted in magenta.