TABLE 1.
Crystallographic analysis and model refinement
| Space group | P21 |
|---|---|
| Unit cell parameters | a = 47.0Å, b = 63.5Å, c = 63.4Å, β = 109.3° |
| Wavelength (Å) | 0.9116 |
| Resolution range (Å) | 50–2.37 |
| Number of observations | 53,672 |
| Completeness (%) | 99.4 (97.5)a |
| Mean I/σ (I) | 22.6 (6.9)a |
| RSYM on Ib | 0.076 (0.216)a |
| Outer resolution shell (Å) | 2.45-2.37 |
| Model and refinement statistics | |
| Resolution range (Å) | 50–2.37 |
| Protein residues (all atoms) | 349 (2,926) |
| Average B-factor (Å2) | 44.0 |
| Unique reflections (test set) | 13,960 (679) |
| Rwork (%)c | 21.6 |
| Rfree (%)d | 26.8 |
| Stereochemical parameters | |
| Observed rms deviations from ideality | |
| Bond lengths (Å) | 0.006 |
| Bond angles (°) | 1.43 |
| Torsion angles (°) | 25.34 |
| Improper torsion angles (°) | 0.74 |
| Ramachandran outliersb | 0.3% |
| Estimated coordinate error | |
| Low resolution cut-off (Å) | 5.0 |
| Luzzati coordinate error (Å) | 0.29 |
| σ A coordinate error (Å) | 0.24 |
a
Outer resolution shell in parentheses.
b
RSYM = ΣIi − 〈Ii〉|/Σ|Ii|, where Ii is the scaled intensity of the ith measurement and 〈Ii〉 is the mean intensity for that reflection.
c
Rwork = Σ||Fo| − |Fc|/Σ|Fo|, where Fc and Fo are the calculated and observed structure factor amplitudes, respectively.
d
Rfree is the same as Rwork, but calculated on the 5% of reflections that were omitted from refinement.