 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 3]](ba5117fig3mag.jpg)
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Figure 3
Determination of the crystal structure of BPV-1 E1 helicase. (a) The AAA+ domain of HPV-18 helicase and (b) the hexamer of SV40 helicase, which were used to generate a synthetic model (c). (d) Refined hexamer. (e) Final structure of BPV-1 E1 helicase. Colours indicate (red) oligomerization and (green) AAA+ domains. The r.m.s.d.s for Cα atoms between the last three models were 5.6 Å (synthetic and final models), 4.5 Å (synthetic and refined models) and 2.5 Å (refined and final models). In the final hexamers the sixfold symmetry is significantly perturbed. Therefore, the r.m.s.d. between the refined and symmetrized final hexamers is only 1.2 Å. (f) The behaviour of MR for synthetic and (g) refined hexamers. RF and TF steps are represented by plots of RF/σ(RF) and by correlation coefficient (CC), respectively, versus RF peak number. |
![[Figure 3]](ba5117fig3.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
