Table 1.
Crystallographic data collection and refinement statistics
| Native 1 | SeMet | Native 2 | |
|---|---|---|---|
| Data collection | |||
| Space group | P212121 | P212121 | P21 |
| Cell dimensions | |||
| a, b, c (Å) | 88.0, 98.1, 112.7 | 89.3, 112.5, 114.4 | 62.0, 111.7, 150.4 |
| α, β, γ (°) | 90, 90, 90 | 90, 90, 90 | 90, 100.6, 90 |
| Wavelength (Å) | 0.9795 | 0.9792 | 0.9792 |
| Resolution (Å) | 2.6 | 2.9 | 3.3 |
| R merge | 0.094 | 0.11 | 0.12 |
| I / σI | 13.3 (1.1)a | 14.3 (1.1) | 8.6 (1.0) |
| Completeness (%) | 99.8 (99.6) | 99.8 (100) | 95 (84) |
| Redundancy | 3.9 (3.8) | 6.0 (5.8) | 3.3 (3.0) |
| Refinement | |||
| Resolution (Å) | 48.9–2.6 | 30.0–2.9 | |
| No. reflections | 29,309 | 24,623 | |
| Rwork / Rfree | 0.208 / 0.258 | 0.223 / 0.278 | |
| No. atoms | |||
| Protein | 6,271 | 6,755 | |
| Water | 53 | 18 | |
| B-factors | |||
| Protein | 75.5 | 116.0 | |
| Water | 79.9 | 119.6 | |
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.014 | 0.014 | |
| Bond angles (°) | 1.594 | 1.765 |
aValues in parentheses are for highest-resolution shell.