Table 2.
Data collection and refinement statistics
| Statistics | AcrIF13 (L66M) | AcrIF13 |
|---|---|---|
| Data collection | ||
| Space group | F23 | F23 |
| Cell dimensions | ||
| a, b, c (Å) | 263.847, 263.847, 263.847 | 262.771, 262.771, 262.771 |
| α, β, γ (°) | 90.00, 90.00, 90.00 | 90.00, 90.00, 90.00 |
| Resolution (Å) | 50–3.03 (3.14–3.03) | 50–2.95 (3.06–2.95)a |
| Rsym or Rmerge (%) | 16.6 (133.7) | 15.7 (169.2) |
| I/σ(I) | 21.2 (2.3) | 30.7 (3.2) |
| Completeness (%) | 99.6 (100.0) | 99.2 (99.9) |
| Redundancy | 31.1 (29.8) | 40.4 (41.3) |
| Refinement | ||
| Resolution (Å) | 50–3.03 | 50–2.95 |
| No. reflections | 29,467 | 31,488 |
| Rwork/Rfree# | 0.2438/0.2843 | 0.2363/0.2705 |
| No. atoms | 7431 | 7425 |
| Protein | 7431 | 7425 |
| Ligand/ion | 0 | 0 |
| Water | 0 | 0 |
| B factors | 72.72 | 54.26 |
| Protein | 72.72 | 54.26 |
| Ligand/ion | ||
| Water | ||
| R.m.s. deviations | ||
| Bond lengths (Å) | 0.006 | 0.008 |
| Bond angles (°) | 0.85 | 1.25 |
| Ramachandran plot (%) | ||
| Favored | 97.17 | 96.84 |
| Allowed | 2.83 | 2.83 |
| Outliers | 0 | 0.33 |
a
For each structure one crystal was used. Values in parentheses are for highest-resolution shell.