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![[Figure 4]](qo5004fig4mag.jpg)
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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 2mFo − DFc (blue) and difference mFo − DFc (red/green) maximum-likelihood maps calculated using REFMAC5 and PDB-REDO are shown at 1.5σ and 3σ levels, respectively. |
![[Figure 4]](qo5004fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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