 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 6]](jb5024fig6mag.jpg)
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Figure 6
Solvent channels in Val58Ile ds-TrpR crystals. (a) View down the long solvent channel. The protein structure was expanded by P6122 symmetry to show the continuous channel through the crystal. Protein helices are represented as gray cylinders. The position of one free N-terminus is marked by a blue arrow at the first ordered residue of the cleaved protein: Ala2 of the native TrpR sequence. L-Trp ligands are shown as CPK spheres in atomic colors with green C atoms. (b) Similar representation as in (a) but with the view rotated ∼45° along the indicated axis. The orange box encloses the area that is enlarged in (c). (c) View of the environment of one L-Trp ligand in Val58Ile ds-TrpR. The symmetry-related L-Trp molecules visible in (b) were deleted for clarity and to match (d). Protein helices are represented as gray ribbons (top) and as solvent-accessible surfaces (bottom). (d) A view equivalent to that in (c) for wild-type dimeric TrpR (PDB entry 1jhg; Lawson, 1996a  ). Note the solvent-accessibility of the L-Trp α-carboxylate functional group. |
![[Figure 6]](jb5024fig6.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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