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![[Figure 9]](ud5026fig9mag.jpg)
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Figure 9
BvHSS variants targeting the tryptophan at the active site. (a) BvHSS variant W229F (PDB entry 6s4d chain A), (b) BvHSS variant W229E (PDB entry 6sep chain B), (c, d) BvHSS variant W229A (PDB entry 6s72 chain A) from different perspectives. (e, f) Superimposition of wild-type BvHSS (PDB entry 4tvb chain B, gray; Krossa et al., 2016  ) onto BvHSS variant W229F (colored) (e) and BvHSS variant W229A (colored) (f). Atomic models are depicted in ball-and-stick representation and electron-density maps as mesh. Large images (a–d) show the 2mFo − DFc maps (black, 1σ) and mFo − DFc maps (green/red, ±4σ) of the complete models. Models lacking the respective exchanged residue together with ten N-terminally and ten C-terminally adjacent residues [I and II in (a–c)] or lacking the PUT molecule [I and II in (d)] were used to calculate (I) 2mFo − DFc omit maps (black, 1σ) and (II) mFo − DFc omit maps (green/red, ±4σ) after refinement including simulated annealing. |
![[Figure 9]](ud5026fig9.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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