journal menu
![[Figure 3]](qo5004fig3mag.jpg)
|
|
Figure 3
Crystal structure of an isolated helix 7 from the N-terminal domain (NTD) of H. pylori DnaB helicase (HpDnaB). Comparison of deposited (a) and corrected (b) models. The peaks in the difference-density mFo − DFc map can be eliminated by shifting the model sequence register by two residues. For example, the clearly too large Phe C/111 resulting in a prominent negative (red) difference-density peak is replaced with a smaller Leu C/113 in the model with the corrected sequence register. Similarly, a clear positive peak (green) near Asn C/115 is interpreted as an Ile C/117 side chain in the corrected model. The combined 2mFo − DFc (blue) and difference mFo − DFc (red/green) maximum-likelihood maps calculated using REFMAC5 and PDB_REDO are shown at 2σ and 3σ levels, respectively. At this threshold no difference-density map features are visible in the presented asymmetric unit fragment of the corrected model. |
![[Figure 3]](qo5004fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
