Table 4 Data collection and refinement statistics* for Y74F and C298S mutants of E. coli Trpase.
From: Conformational changes and loose packing promote E. coli Tryptophanase cold lability
| Y74F [PDB:2V1P] | C298S [pdb:2V0Y] | |
|---|---|---|
| Data collection | ||
| Space group | F222 | F222 |
| Wavelength | 1.5Å | 1.5Å |
| Unit cell | a = 118.7Å | a = 120.5Å |
| b = 120.2Å | b = 118.8Å | |
| c = 171.7Å | c = 171.5Å | |
| α = 90° | α = 90° | |
| β = 90° | β = 90° | |
| γ = 90° | γ = 90° | |
| Resolution | 500.0-1.90 Å | 500.0-1.98 Å |
| Highest resolution shell | 1.97-1.90 Å | 2. 05-1.98 Å |
|
Total number of measured reflections Total number of independent reflections |
155,699 47,181 |
186,657 42,496 |
| Completeness (%) | 97.6% (97.8%) | 99.3% (96.5%) |
| Rsym | 0.054 (0.410) | 0.117 (0.456) |
| I/σ (I) | 19.0 (2.9) | 12.7 (2.9) |
| Refinement | ||
| Resolution range (Å) | 6.0-1.9 | 8.0-2.0 |
| R (%) | 19.14 | 21.48 |
| Rfree (%) | 22.72 | 22.09 |
| Protein atoms | 3682 | 3678 |
| Solvent atoms | 595 | 519 |
| Mg2+ atoms | 1 | 1 |
| Cl- atoms | 1 | 1 |
| RMS deviations from restraints target value | ||
| Bond length (Å) | 0.005 | 0.006 |
| Bond Angle (°) | 1.21 | 1.22 |
|
Average B factor (for protein atoms) (Å2) | 28.8 | 28.9 |
