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![[Figure 4]](cb5053fig4mag.jpg)
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Figure 4
Snapshot of O-esterase catalysis in crystallo. Trapping of a covalent acyl-enzyme intermediate. All 2Fo − Fc and Fo − Fc electron-density maps surrounding Ape1 residues or acetate are contoured at 1.2σ for 2Fo − Fc maps and at ±3.0σ for Fo − Fc maps. 0 min: the active site of native Ape1. 5 min, chain A: trapped acetate group coloured purple. 5 min, chain B: trapped acyl-enzyme intermediate coluored purple. 30 min, chain A/B: trapped water molecules in the active site of Ape1. See 0 min for complete labelling of the active-site residues. |
![[Figure 4]](cb5053fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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