view article

Figure 4
Crystal structure of HydF maturase with a register-shifted fragment of a GTP-binding domain shown in red (a). The dashed circle indicates the region of the deposited model shown in (b) with the corresponding electron-density maps. Asp B/176 is a clear map–model fit outlier that results in a strong negative peak in the difference-density map and a register shift in the fragment shown in red in (a). The remaining three HydF chains in the asymmetric unit superimposed onto chain B are shown in grey. After correcting the model and subsequent restrained refinement the map–model agreement clearly improves (c). The combined 2mFoDFc (blue) and difference mFoDFc (red/green) maximum-likelihood maps calculated using REFMAC5 and PDB-REDO are shown at 1.5σ and 3σ levels, respectively.

Journal logoSTRUCTURAL
ISSN: 2059-7983
Follow Acta Cryst. D
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds