Table 1.
Crystallographic data and refinement statistics
| Crystallographic data | Closed form | Open form |
|---|---|---|
| Reference | Dekker et al., 2011 | Muñoz et al., 2011 |
| Space group | P1 | P21212 |
| Unit cell parameters | a=159.10Å | a=272.7Å |
| b=162.54Å | b=313.5Å | |
| c=268.10Å | c=158.3Å | |
| α=85.23° | ||
| β=81.15° | ||
| γ=61.17 | ||
| Wavelength (Å) | 1.00 | 1.114 |
| Resolution range (Å) | 90.0-3.8 | 100.0-5.5 |
| Completeness (%) | 91.6 (93.2)a | 92.5 (95.3)a |
| Mean I/σ(I) | 8.4 (1.92)a | 9.54 (1.2)a |
| Highest resolution shell (Å) | 4.0-3.8 | 6.0 - 5.5 |
| Refinement | ||
| Resolution range (Å) | 90.0-3.8 | 100.0-5.5 |
| No. of reflections (total / for Rfree) | 209671 / 10483 | 44462 / 2238 |
| Rwork / Rfree | 0.2479 / 0.2837 | 0.340 /0.398 |
| Average isotropic | 131.4 | 277.3 |
| B-factor (Å2) | ||
| Number of residues Protein | 32 chains | 16 chains |
| 16716 structured residues (95.5% of all residues) b | 6842 structured residues (78.8% of all residues) | |
| ADP | 32b | |
| BeF3 | 32b | |
| Mg2+ | 32b | |
| RMS deviation | ||
| Bond angle RMSD (°) | 1.62 | 0.65 |
| Bond length RMSD (Å) | 0.0128 | 0.002 |
| Ramachandran statistics (%) | ||
| Favored | 80.3 | 87.1 |
| Allowed | 15.5 | 10.7 |
| Outliers | 4.2 | 2.1 |
a
in the highest resolution shell.
b
NCS constraints enforced between the four octameric rings in the asymmetric units.