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Figure 5.
Fig. 5. (a) Maps showing the binding of C[6]F[5]I to
selenium-substituted L99A. The isomorphous difference map has
amplitudes (F[obs,complex] – F[obs,L99A]) and phases from the
refined structure of L99A. It is shown in red, and contoured at
3.0σ. C[6]F[5]I has density for the bound ligand and, due to
the replacement of Met102, with the more electron-dense
selenomethionine (top left). The map based on the anomalous
scattering differences, contoured in green, is contoured at
3.0σ. (b) Electron density maps, as in panel a, for C[6]H[5]I
bound to selenomethionine L99A. The ligand occupies the position
shown as well as one rotated 180°.
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