 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 6]](gr2165fig6mag.jpg)
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Figure 6
Bias in prime-and-switch phasing. Model data sets with varying solvent contents and `molecular-replacement' models with atomic coordinates differing from the perfect models by an r.m.s.d. of 1.4 Å were constructed as described in the text. Phases were calculated with σA weighting and with prime-and-switch phasing. The prime-and-switch phasing was carried out beginning with the σA-weighted phases; ten cycles of solvent-mask identification each with 40 iterations of phasing were carried out. In all cases, essentially complete convergence was achieved within this number of cycles. In (a), the normalized electron density in the σA-weighted map (open circles) or prime-and-switch phased map (closed circles) at coordinates of atoms in the perfect model are shown. Additionally, the normalized electron density in the σA-weighted map (open squares) or prime-and-switch phased map (closed squares) at coordinates of incorrectly placed atoms in the molecular-replacement model used for phasing are shown. In (b), the ratio of the electron density at incorrectly placed atoms to correctly placed atoms is shown for the σA-weighted map (open circles) or prime-and-switch phased map (closed circles). |
![[Figure 6]](gr2165fig6.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
