 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 2]](gr2164fig2mag.jpg)
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Figure 2
Experimental, real-space density-modified, maximum-likelihood density-modified and maximum-likelihood with pattern-recognition modified maps of an α-helical protein. The armadillo repeat region of β-catenin crystallizes in space group C2221, with unit-cell parameters a = 64, b = 102, c = 187 Å and a solvent content of about 50% (Huber et al., 1997  ). Phases were calculated with SOLVE (Terwilliger & Berendzen, 1999) using three selenium sites at a resolution of 3 Å. A section of this map is shown in (a). Real-space density modification was carried out with DM (Cowtan & Main, 1996) using solvent flattening with a solvent content of 50% and histogram matching (not shown). Maximum-likelihood density modification without image reconstruction was carried out as described earlier (Terwilliger, 2000) using a solvent content of 50% (b). Templates found in the experimental electron-density map are illustrated in (c). Maximum-likelihood density modification with pattern recognition was carried out as described in the text, using a solvent content of 50% and a fraction helical secondary structure of 80% (d). Template matches with a probability less than 0.8 were not included. |
![[Figure 2]](gr2164fig2.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
