 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 3]](rr5069fig3mag.jpg)
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Figure 3
Test xMDFF refinement of the `closed' conformation of D-ribose-binding protein using its `open' conformation as the initial phasing model. Starting with an initial model of the open conformation (PDB entry 1urp ; cyan) of the D-ribose-binding protein (a) and diffraction data from the target closed structure (PDB entry 2dri ; orange) at resolutions ranging from 3.5 to 5 Å, xMDFF refinements were performed. (b) The xMDFF-refined closed structure (red) shows excellent agreement with the target at all resolutions (5 Å resolution shown with a final Rfree of 0.34, down from an initial 0.56). Overall improvement was characterized using the Rfree and cross-correlation of the final xMDFF structure and the r.m.s.d. of the final xMDFF structure to the target. Structural refinement is suggested by all three measures as well as the all-atom statistics provided in Table 1 ![[link]](../../../../../../logos/arrows/d_arr.gif) . |
![[Figure 3]](rr5069fig3.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
