 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
journal menu
![[Figure 5]](dz5074fig5mag.jpg)
|
|
Figure 5
Electron-density maps showing the improvement of phase information as the structure was being completed and experimental phase information introduced. All panels show residues 540–565 from the D2 domain of the A chain of VCP/p97–ADP·AlFx using the coordinates of the final model (green). Also shown in all panels is an anomalous difference map computed from a data set collected at the selenium edge of a selenomethionine-substituted protein crystal, contoured at 4σ (red). Superimposed are σA-weighted 2Fo − Fc maps calculated to 4.5 Å and displayed at a 1σ contour level (blue). All images are shown in cross-eyed stereo with every fifth residue number indicated. (a) Fc and phases for this map were taken from the molecular-replacement solution using the N–D1 model (∼60% of the complete model, i.e. no information about the D2 domain was used at this point). (b) Phase-combined map. Model structure-factor phases for this map were taken from a model based on a minimized N–D1 region with the D2 region built as a discontinuous polyserine trace. The 6.5 Å MAD phases were combined with the model phases. (c) Phase-combined map using the final model. This map has neither optimized bulk-solvent correction nor B-factor sharpening applied to it. (d) As (c), but with optimized bulk-solvent model and B-factor sharpening. |
![[Figure 5]](dz5074fig5.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
