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Figure 5
Comparison of various refinements and maps for residues 251–276. Residues 251–263 comprising an α-helix, residues 264–271 comprising a loop and residues 272–276 comprising a β-strand are shown (the sequence numbers refer to the genomic sequence; see Fig. 1[link]). (a) Standard refinement (gray) versus the final model (orange). Standard refinement produces fragmented or incorrectly connected electron density (marked by arrows). (b) Standard refinement and one round of AutoBuild (blue) versus the final model (orange). Electron density is still fragmented or shows incorrect connectivity. (c) DEN refinement (green) versus the final model (orange). (d) DEN refinement and one round of AutoBuild (magenta) versus the result of semi-automated rebuilding (yellow). (e) 2mFoDFc electron-density map after standard refinement (blue mesh) and a subsequent round of AutoBuild (cyan mesh) versus the final structure (orange sticks). (f) 2mFo − DFc electron-density map after DEN refinement (blue) and a subsequent round of AutoBuild (cyan) versus the final structure (orange sticks). (g) Electron-density map obtained by density modification of the MAD map (blue) versus the final structure (orange sticks). (h) 2mFo − DFc electron-density map (blue mesh) of the final model (orange sticks).

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
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