Table 1.
Data collection and refinement statistics for the QF, GGY, and YT mutants of PTE.
| Enzyme | H254Q H257F |
I106G F132G H257Y |
H257Y L303T |
|---|---|---|---|
| Data Collection | |||
| Space Group | P1 | P1 | P1 |
| Cell Dimension | |||
| a, b, c (Å) | 43.53, 45.37, 79.11 | 56.76, 68.91, 89.67 | 43.36, 45.37, 79.21 |
| α, β, γ (°) | 104.75, 93.13, 97.97 | 90.03, 100.29, 94.12 | 104.86, 93.27, 97.81 |
| Resolution (Å) | 50.0–1.80 (1.86-1.80) | 50.0–1.58 (1.64-1.58) | 50.0–1.04 (1.08-1.04) |
| I/σ | 12.9 (3.0) | 10.2 (1.5) | 17.3 (6.3) |
| Completeness (%) | 91.8 (70.2) | 93.1 (73.5) | 85.5 (41.4) |
| Redundancy | 1.9 (1.8) | 1.9 (1.7) | 3.4 (2.6) |
| Rmerge | 0.055 (0.245) | 0.075 (0.397) | 0.061(0.188) |
| Refinement | |||
| Observed Reflections | 49,147 | 155,682 | 235,873 |
| Protein Nonhydrogen Atoms | 5,174 | 10,277 | 5,178 |
| Water Molecules | 700 | 1,636 | 855 |
| Rwork | 0.146 | 0.189 | 0.105 |
| Rfree | 0.189 | 0.244 | 0.127 |
| Average B-factor, (Å2) | 14.48 | 19.87 | 9.99 |
| RMSD from Ideal Geometry | |||
| Bond Length (Å) | 0.013 | 0.016 | 0.015 |
| Bond Angles (°) | 1.4 | 1.6 | 1.5 |