Figure 1 : Design of the stringent starvation protein B (SspB)-fusion protein.

From: ACCORD: an assessment tool to determine the orientation of homodimeric coiled-coils

Figure 1

(a) Overall structure of the SspB protein. The tail residues from 112 to 165, shown in dots, were not modelled because of their flexibility. The distance between Asp111 and Asp111′ is approximately 40 Å. The N-terminal hexa-histidine tag is shown as a red block. (b) Domain architecture of the SspB-CCD fusion protein. The N-terminal hexa-histidine tag, full-length SspB (residues 1 to 165), and target coiled-coil domain (CCD) are coloured red, green, and blue, respectively. (c) Schematic model of a dimer of SspB fused with a parallel CCD. The N- and C-termini of the CCs are indicated. (d) Schematic model of a possible arrangement of a tetramer of SspB fused with an antiparallel CCD. The N- and C-termini of the CCs are indicated. (e) A possible arrangement of higher-order oligomers of SspB fused with an antiparallel CCD and protein aggregation during concentration of the sample (left: soluble control protein; right: aggregation of higher-order oligomers).