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![[Figure 4]](ag5025fig4mag.jpg)
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Figure 4
Atomic ordering of the YfeA flexible lobe. The holo YfeA reconstitution experiment reveals atomic ordering of flexible lobe helix 7. (a, b) Enlarged images showing the model overlaid with anomalous difference electron density contoured at 5σ (magenta mesh) and electron density calculated from a 2Fo − Fc map contoured at 1σ (blue mesh). The Zn atom is omitted to emphasize the increase in anomalous difference electron density across soaks, and the site 1 placeholder water molecule (red sphere) and residues (gray sticks) are shown. In the apo structure (a) (green), 2042 out of 2153 protein atoms are modeled and there is a visible gap between two flexible lobe residues where Pro226–Val238 should be. In the reconstituted holo structure (b) (yellow), with the spring-hammer having engaged the Zn atom, all amino acids are resolved as 2153 out of 2153 protein atoms are modeled. |
![[Figure 4]](ag5025fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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