Table 1.
Data collection and refinement statistics
| Data collection | |
| Space group | P3221 |
| Cell dimensions | |
| a, b, c (Å) | 407.42, 407.42, 808.63 |
| α, β, γ (deg) | 90.0, 90.0, 120.0 |
| Resolution (Å) | 80.0–3.4 (3.6–3.4)a |
| Rsym or Rmerge | 24.0 (52.6)a |
| I/σI | 3.3 (1.0)a |
| Completeness (%) | 69.9 (41.6)a |
| Redundancy | 1.5 (1.3)a |
| Refinement | |
| Resolution (Å) | 50.0–3.4 |
| No. of reflections | 736678/3758 |
| Rwork/Rfree b | 27.2/27.3 |
| No. atoms | |
| Protein | 8234 |
| Water | 52 |
| B-factors | |
| Protein | 34.1 |
| Water | 5.0 |
| RMS deviations | |
| Bond lengths (Å) | 0.010 |
| Bond angles (deg) | 1.5 |
aValues in parentheses are for highest-resolution shell.
bRfree value calculated with 0.5% of the relflections data set, selected by resolution shells. Because of the high redundancy in the data set due to a 30-fold non-crystallographic symmetry, the Rfree does not represent a ‘free' set, hence the very small difference with the working R. To avoid over-fitting, refinement was therefore carried out with a high weight to the geometry of the model, and the NCS were maintained as constraints throughout, to reduce the number of parameters to be fitted.