Figure 4.

Comparison of the experimental electron-density maps from SOLOMON (a) and RESOLVE (b) contoured at 1σ. The SOLOMON solvent-flattened electron-density map was calculated at 4 Å resolution and allowed the identification of clear protein and solvent boundaries. Secondary-structure elements are readily interpretable in the 2.9 Å resolution RESOLVE solvent-flattened and NCS-averaged map. The map skeleton is shown (in yellow) to highlight map connectivity in both figures. The anomalous substructure map in magenta (contoured at 3σ) indicates the location of Ta₆Br₁₂ clusters.