FIGURE 3.

Sequence conservation of dmCstF-50N. (A,B) dmCstF-50N is a phylogenetically conserved homodimer. dmCstF-50N is depicted under a similar orientation as in Figure 1 with one monomer as a cartoon, whereas the other monomer is shown as a surface representation. Residues involved in homodimer formation in cartooned monomer are labeled. On the right, the cartoon representation of one monomer has been omitted to expose its conserved fingerprint on the other monomer. Sequence conservation is shown from white to red ranging from nonconserved to conserved residues. This figure has been produced using ESPript program (Gouet et al. 2003). Conserved residues involved in protein–protein interaction are labeled. Some secondary structure elements are shown underneath. (C,D) A PEG molecule sits in a conserved surface area of the complex. A PEG molecule coming from the crystallization condition can be modeled into the conserved cavity at the surface of dmCstF-50N. Residue conservation has been calculated as described in Figure 2. The Fobs-Fcalc electron density map contoured at 1.5 σ around the PEG molecule in shown as a blue mesh. Conserved residues are labeled.