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. 2012 Sep 18;68(Pt 10):1371–1379. doi: 10.1107/S0907444912029599

Figure 3.

Figure 3

(a) Stereo pair of an electron-density map (1.0σ) calculated with the starting experimental phases after density improvement with AUTOSOLVE (Zwart et al., 2008 ▶). The manually placed three-helix bundle is shown as a yellow tube model; the threefold crystallographic axis is indicated by a red line. (b) The white mesh represents the same map as shown in (a). The purple map was calculated from phases that were improved using PARROT. Manually placed secondary-structure elements are represented by yellow tubes. (c) The purple mesh is the same as in (b). The green map was calculated after cross-crystal averaging between the 3.5 Å resolution data set and the 4.2 Å resolution data set (Table 2 ▶) using DMMULTI (Winn et al., 2011 ▶). Manually placed secondary-structure elements are represented by yellow tubes. The crystal structure (white tubes) of the SAM-dependent methyltransferase from Pyrococcus horikoshii OT3 (PDB entry 1wzn; RIKEN Structural Genomics/Proteomics Initiative, unpublished work) is superimposed onto the manually placed secondary-structure elements. (d) The green mesh is the same as in (c). The individual domains of WbdD556 are indicated (white, methyltransferase domain; red, kinase domain; yellow, three-helix bundle).