Table 1.
Data collection and refinement statistics
| Wavelength (Å) | 0.9797 |
| Resolution (Å) | 12–2.5 |
| Temperature (K) | 113 |
| Space group | I422 |
| Cell dimensions | |
| a (Å) | 208.597 |
| c (Å) | 136.358 |
| No. of molecules per asymmetric unit | 6 |
| No. of unique reflections | 51,262 |
| Rsym (%)a,b | 8.2 (44.2) |
| Completeness (%) | 98.9 (90.3) |
| Redundancies | 7.3 |
| I/σ (I) | 20.5 (2.7) |
| Refinement statistics | |
| Resolution range | 12–2.5 |
| No. of reflections used in refinement | 46,761 |
| σ cutoff used in refinement | 0 |
| R/Rfree (%)c | 18.32/23.04 |
| Number of refined atoms | |
| Protein | 6613 |
| Heterogen atoms | 92 |
| Water | 348 |
| Average B-factors (Å2) | |
| Protein | 30.5 |
| Sulphate anions | 41.9 |
| Glycerol | 33.3 |
| Water | 46.4 |
| R.m.s. deviations | |
| Bonds (Å) | 0.016 |
| Angles (°) | 1.672 |
a Values in parentheses are for the highest-resolution shell.
bRsym = ∑|Ii - 〈Ii〉|/∑Ii, where Ii is the intensity of the ith observation and 〈Ii〉is the mean intensity of the reflection.
cR = ∑||Fo | - ||Fc||/∑|Fo|, where Fo and Fc are the observed and calculated structure factors amplitudes. Rfree is calculated by using 3.0% of reflections omitted from the refinement.