|
Figure 4.
Fig. 4. The crystal structure of W136A mutant. (a) Electron
density, contoured at 1.5σ level, at the site of mutation.
Water molecules are shown in red, and detergents in green. (b)
The water molecules (numbered 1 to 6) substituting the indole
ring of Trp136 are stabilized by a network of hydrogen bonds.
(c) The structure of the wild type showing the interfacial
location of Trp136. (d) After mutation, the protein surface is
no longer compatible with its buried location.
|
