 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 4]](gr0866fig4mag.jpg)
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Figure 4
Standard deviation of local r.m.s. electron density during structure determination of Rhodococcus dehalogenase. The structure solution of Rhodococcus dehalogenase was carried out using the program SOLVE (Terwilliger & Berendzen, in preparation) based on data from a native and five derivatives (Au, Au, Hg, Pt and Sm heavy atoms) with anomalous differences measured for each derivative (J. Newman, unpublished data). SOLVE evaluated a total of 186 potential heavy-atom solutions during the course of structure determination. Each heavy-atom solution was compared with the final solution and an origin shift or inversion was applied if necessary to match the heavy-atom positions. As discussed in the text, (a) shows only solutions with the correct hand and (b) compares matching solutions with inverted handedness. (a) Non-randomness of native Fourier versus map quality. The abscissa is the standard deviation of the local r.m.s. electron density in the test native Fourier. The ordinate is the correlation coefficient between the native Fourier calculated from the trial-refined heavy atoms and the final refined model of the dehalogenase. (b) Non-randomness of the native Fourier as a function of the number of correct heavy-atom sites in test solutions for solutions of correct or inverted hand. The abscissa is the total number of correct heavy-atom sites in the five derivatives used in phasing, where a site was considered correct if it was within 1.5 Å of a heavy-atom site in the final solution in the appropriate derivative. The ordinates are the standard deviations of local r.m.s. density for native Fouriers calculated with correct and inverted handedness. |
![[Figure 4]](gr0866fig4.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
