Table 1.
Crystallographic data collection and refinement statistics.
| Conformation ligand | Closed Ap5A | Open |
|---|---|---|
| Data collection | ||
| Space group | P1 | P21 |
| Cell dimensions | ||
| a, b, c (Å) | 39.20, 48.34, 52.57 | 44.22, 53.7, 50.87 |
| α, β, γ (°) | 75.30, 72.95, 88.77 | 90, 114.46, 90 |
| Resolution (Å) | 1.48 (1.51–1.48)⁎ | 1.70 (1.73 – 1.70) |
| Rr.i.m.a | 0.070 (0.304) | 0.093 (0.104) |
| Rp.i.m.a | 0.049 (0.215) | 0.051 (0.054) |
| I/σI | 25.27 (5.97) | 7.97 (6.80) |
| Completeness (%) | 93.11 (87.46) | 97.84 (98.72) |
| Redundancy | 3.7 (3.4) | 3.5 (3.4) |
| Refinement | ||
| Resolution (Å) | 50 – 1.48 | 25.05 – 1.69 |
| No. reflections | 54,770 | 23,924 |
| Rwork/Rfree | 0.195/0.226 | 0.180/0.222 |
| No. atoms | 7,379 | 2,035 |
| Protein | 3,336 | 1,674 |
| Ligand/ion | 116 | 5 |
| Water | 583 | 356 |
| B-factors | 37.60 | 14.40 |
| Protein | 36.50 | 12.60 |
| Ligand/ion | ||
| Water | 46.00 | 22.80 |
| R.m.s. deviations | ||
| Bond lengths (Å) | 0.009 | 0.019 |
| Bond angles (°) | 1.39 | 1.79 |
| Ramachandran plot | ||
| Most favored regions (%) | 95.1 | 95.2 |
| Additional allowed regions (%) | 4.9 | 4.8 |
⁎
Values in parentheses are for the highest-resolution shell.
a
Rr.i.m., redundancy-independent merging R factor; Rp.i.m., precision-indicating merging R factor [45].