Figure 2 - full size

 

Figure 2.
Figure 2. Structures of the KcsA selectivity filter solved in a high concentration of K^+ (a), Rb^+ (b), Tl^+ (c), and a low concentration of K^+ (d). The structures solved in the absence of TBA are colored in yellow (PDB code 1K4C (a), 1R3I (b), 1R3J (c) and 1K4D (d)). The structures solved in the presence of TBA are colored in red, covered with F[o]–F[c] omit map (blue, contoured at 3σ ((a), (b) and (d)) or 2.5 σ (c)). The maps are calculated using a model with both the filter (residues T74 to G79) and ions removed. The pink electron density maps are F[o]^TBSb–F[o]^TBA difference maps countered at 10σ for (a) and (c), 18σ for (b), and 12 σ for (d). Figure 2. Structures of the KcsA selectivity filter solved in a high concentration of K^+ (a), Rb^+ (b), Tl^+ (c), and a low concentration of K^+ (d). The structures solved in the absence of TBA are colored in yellow (PDB code 1K4C (a), 1R3I (b), 1R3J (c) and 1K4D (d)). The structures solved in the presence of TBA are colored in red, covered with F[o]–F[c] omit map (blue, contoured at 3σ ((a), (b) and (d)) or 2.5 σ (c)). The maps are calculated using a model with both the filter (residues T74 to G79) and ions removed. The pink electron density maps are F[o]^TBSb–F[o]^TBA difference maps countered at 10σ for (a) and (c), 18σ for (b), and 12 σ for (d).

The above figure is reprinted by permission from Elsevier: J Mol Biol (2007, 366, 806-814) copyright 2007.