Table 1. Data-collection and structure statistics.
Values in parentheses are for the highest resolution shell.
| Data collection | |
| Wavelength (Å) | 0.9791 |
| Space group | C2 |
| Unit-cell parameters (Å, °) | a = 134.11, b = 73.51, c = 34.60, β = 96.52 |
| Resolution (Å) | 35.00–2.00 (2.07–2.00) |
| Rmerge† | 0.136 (0.310) |
| 〈I/σ(I)〉 | 18.5 (7.2) |
| Completeness (%) | 98.1 (97.4) |
| Multiplicity | 14.6 (14.3) |
| Mosaicity (°) | 0.9 |
| No. of crystals | 1 |
| Temperature (K) | 100 |
| Oscillation (°) | 1 |
| Rotation range (°) | 680 |
| Exposure per frame (s) | 4 |
| Crystal-to-detector distance (mm) | 200 |
| Detector | MAR325 |
| Refinement | |
| No. of reflections | 20817 |
| Rwork/Rfree | 0.22/0.26 |
| No. of atoms | |
| Protein | 1142 [chain A], 1142 [chain B] |
| Ligand/ion | 2 Ca, 4 ACT |
| Water | 288 |
| B factors (Å2) | |
| Protein | 17.3 [chain A], 18.3 [chain B] |
| Ligand/ion | 30.3 [Ca], 31.4 [ACT] |
| Water | 31.2 |
| R.m.s. deviations | |
| Bond lengths (Å) | 0.010 |
| Bond angles (°) | 1.252 |
| Ramachandran plot (%) | |
| Favoured | 86.9 |
| Allowed | 13.1 |
| Outliers | 0.0 |
†
R
merge = 
, where Ii(hkl) is the ith observation of reflection hkl and 〈I(hkl)〉 is the weighted average intensity for all observations i of reflection hkl.