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Figure 6
(a) The active site of S. coelicolor DHQase with 16-fold averaged weighted difference electron density corresponding to the inhibitor CA1 (the position of the unrefined model is shown in ball-and-stick representation), clearly showing the stereochemistry of the bifunctional inhibitor. Additional density corresponds to ordered water molecules in the active site of the enzyme. (b) The final unaveraged electron density contoured at 2σ for the active site of a representative monomer within the structure.

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047
Volume 64| Part 1| December 2008| Pages 108-118
doi:10.1107/S0907444907054923
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