Table 1.
Crystallographic data collection and refinement.
| BBRF2Δ | BBRF2Δ-BSRF1Δ complex | |
|---|---|---|
| Data collection | ||
| Space group | P21212 | P21 |
| Cell dimensions | ||
| a, b, c (Å) | 73.318, 61.571, 58.109 | 75.78, 161.85, 97.86 |
| α, β, γ (°) | 90, 90, 90 | 90, 100.8, 90 |
| Wavelength (Å) | 0.97915 | 0.97853 |
| Resolution (Å)a | 47.15–1.6 (1.69–1.6) | 48.07–3.09 (3.28–3.09) |
| Total reflections | 248,156 (39,396) | 145,743 (21,580) |
| Unique reflections | 66,863 (10,656) | 42,196 (6720) |
| Rsym | 0.072 (0.575) | 0.082 (0.495) |
| I/σ(I) | 13.39 (3.98) | 13.27 (2.23) |
| Completeness (%) | 99.1 (97.5) | 99.4 (98.3) |
| Redundancy | 3.71 (3.7) | 3.45 (3.21) |
| Refinement | ||
| Rwork/Rfree | 0.166/0.189 | 0.217/0.27 |
| No. of atoms | ||
| Protein | 2153 | 16,133 |
| Ligand/ion | 14 | 30 |
| Water | 278 | 28 |
| B-factors | ||
| Protein | 23.15 | 75.67 |
| Ligand/ion | 56.60 | 65.38 |
| Water | 37.23 | 44.86 |
| R.m.s. deviations | ||
| Bond lengths (Å) | 0.009 | 0.009 |
| Bond angles (°) | 1.11 | 1.10 |
| Ramachandran | ||
| Favoured (%) | 98.5 | 92.0 |
| Outliers (%) | 0 | 1.1 |
aNumbers in parentheses are values from the highest resolution shell.