Table 1.
Diffraction data statistics and model refinement parameters.
| space group | P21 |
| unit cell dimensions | a = 70.79 Å, b = 24.41 Å, c = 75.39 Å, β = 107.65° |
| X-ray data | |
| beamline | I03 (diamond) |
| detector | ADSC Q315r |
| wavelength (Å) | 0.97 |
| resolution (Å) | 20.00–2.10 (2.15–2.10) |
| no. unique reflections | 14 626 (1008) |
| Rsym (I) | 2.7 (45.0) |
| multiplicity | 3.64 (3.74) |
| completeness (%) | 97.7 (99.3) |
| I/σ (I) | 17.24 (3.31) |
| model refinement | |
| no. reflections in working/free set | 13 899/725 |
| no. protein residues | 228a |
| no. solvent molecules/buffer molecules | 55/20b |
| R-factor/R-free (%) | 21.18/26.15 |
| RMSD bond length (Å)/bond angle (°) | 0.006/0.836 |
| Ramachandran statistics | |
| favoured/allowed/outliers (%) | 99.07/0.46/0.47 |
aOut of a total of 244 amino acids, 16 residues were structurally disordered and are missing from the model (corresponding to 6.5% of the structure). The missing residues are as follows: chain A (G271), chain C (G-3, E269, P270, G271), chain B (E269, P270, G271), chain D (G-3, A-2, M-1, D214, D268, E269, P270, G271).
bOrdered buffer components are glycerol and acetic acid.