 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](rr5069fig1mag.jpg)
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Figure 1
xMDFF re-refinement characteristics for six structures. The structures with diffraction data between 4 and 4.5 Å resolution had been deposited earlier in the Protein Data Bank and were used as initial models for xMDFF refinement. Improvements were evaluated using the Rfree values of the xMDFF-refined structures (shown in red) against their respective starting values taken from the deposited structure (blue). In addition, the increase in the percentage of favored Ramachandran angles owing to xMDFF refinement and other structural statistics, as summarized by the overall MolProbity score, were used to measure the improvement in structural geometries. Further details of the refined structures are provided in Table 1 ![[link]](../../../../../../logos/arrows/d_arr.gif) . |
![[Figure 1]](rr5069fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
