Table 1.
Data collection and refinement statistics
| IniA (Pt derivative) | IniA (GTP-bound) | IniA (nucleotide-free) | |
|---|---|---|---|
| Data collection | |||
| Space group | P64 | P64 | P31 |
| Cell dimensions | |||
| a, b, c (Å) | 91.15, 91.15, 139.39 | 91.51, 91.51, 139.49 | 91.76, 91.76, 137.34 |
| α, β, γ (°) | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 |
| Wavelength (Å) | 0.9779 | 0.9779 | 0.9785 |
| Resolution (Å) | 50.00–2.60 (2.64–2.60)a | 50.00–2.20 (2.24–2.20) | 50.00–3.20 (3.26–3.20) |
| Completeness (%) | 100.0 (100.0) | 100.0 (100.0) | 99.9 (100.0) |
| Rmerge (%) | 13.7 (73.7) | 13.1 (53.9) | 19.0 (81.3) |
| Redundancy | 10.3 (10.3) | 20.6 (21.2) | 5.2 (5.3) |
| I/σ(I) | 19.5 (3.0) | 25.4 (4.0) | 7.4 (1.9) |
| Refinement | |||
| Resolution (Å) | 46.50–2.20 | 39.73–3.21 | |
| No. of reflections | 33,560 | 21,086 | |
| Rwork/Rfree (%) | 18.5/22.1 | 21.9/25.8 | |
| No. of atoms | |||
| Protein | 4343 | 8375 | |
| Ligand | 43 | ||
| Water | 333 | ||
| B-factor (Å2) | |||
| Protein | 48.92 | 55.42 | |
| Ligand | 51.93 | ||
| Water | 48.19 | ||
| R.m.s deviations | |||
| Bond lengths (Å) | 0.004 | 0.012 | |
| Bond angles (°) | 0.844 | 2.127 | |
| Ramachandran plot (%) | |||
| Favored | 97.1 | 97.7 | |
| Allowed | 2.7 | 2.1 | |
| Outliers | 0.2 | 0.2 | |
aValues in parentheses are for highest-resolution shell