Table 2. Data collection and refinement statistics.
| Space group | I23 | |
| Cell dimensions | a, b, c (Å) | 89.95, 89.95, 89.95 |
| Wavelength (Å) | 0.9395 | |
| Resolution (Å) | 25.00–1.3 (1.3–1.37) | |
| Measured reflections | 3427903 | |
| Unique reflections | 38741 | |
| Rmerge | 0.069 (0.295) | |
| I/σI | 6.1 (2.2) | |
| Completeness (%) | 99.0 (100.0) | |
| Redundancy | 13.9 (14.2) | |
| Wilson B factor (Å2) | 12.2 | |
| Rcryst (N° reflections) | 0.14 (29381) | |
| Rfree (N° reflections) | 0.17 (1509) | |
| No. atoms | Protein | 4960 |
| Water | 172 | |
| B-factors | Protein | 32.32 |
| Water | 33.89 | |
| R.m.s deviations | Bond lengths (Å) | 0.005 |
| Bond angles (°) | 1.09 |
Numbers in parentheses refer to the highest resolution shell. Rmerge = Σ|I _ 〈I〉|/〈ΣI〉, where I = observed intensity. Rcryst = Σ|Fo _ Fc|/Σ|Fo|, where |Fo| = observed structure factor. Amplitude and |Fc| = calculated structure factor amplitude. Rfree is Rcryst for 3% of reflections excluded from the refinement.