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![[Figure 4]](xh5067fig4mag.jpg)
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Figure 4
Snapshots of the UOX active site with its bound ligands at different dose points for the 100 K and RT experiments. The UOX active site is contributed by two subunits, shown here as stick representations in cyan and magenta. In all panels the mFo − DFc electron-density map is shown around the ligands as a green mesh displayed at the +3σ level. Ligands are shown for reference. (a) The 5-PMUA adduct is largely intact at 100 K and low X-ray dose (2.34 kGy). (b) A similar view at RT and low dose (2.50 kGy), showing the 5-PMUA species. (c) At high X-ray dose (373 kGy) at 100 K, the C5–Op1 bond is incompletely cleaved, with dioxygen (O2) trapped in the active site due to the `cage effect' at cryogenic temperatures, which is critical for its partial regeneration. (d) At RT (72.50 kGy), 5-PMUA is fully broken; O2 has escaped and is replaced by a water molecule (W1) located above the MUA radical. |
![[Figure 4]](xh5067fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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