TABLE 1.
Summary of diffraction data and structure refinement statistics
| Parameter | Value or description |
|---|---|
| No. of crystals | 6 |
| No. of images | 276 |
| Crystal system/space group | Orthorhombic/I222 |
| Cell parameters a, b, and c (Å) | 339.6, 319.2, 285.0 |
| Resolution range (Å) | 50-3.2 |
| No. of unique reflections | 192,100 |
| Rsym (%)a | 16.4 (42.6)d |
| Completeness (%) | 75.9 (42.6)d |
| Rfactorb | 0.263 |
| Rfreec | 0.273 |
| RMSD for bond length (Å)/RMSD for angles (°) | 0.008/1.601 |
| Total no. of protein/nucleotide/ solvent atoms | 4129/22/15 |
| Average B factor for protein/nucleotide/ solvent atoms (Å2) | 30.8/54.7/8.0 |
| Ramachandran plot statistics (most favored/additionally allowed/ generously allowed) (%) | 75.8/22.6/1.6 |
a
Rsym = ΣI − <I>/Σ<I>, where I is the intensity of a reflection with indices h, k, and l and <I> is the average intensity of all symmetry-equivalent measurements of that reflection.
b
Rfactor = Σ|Fo − Fc|/ΣFo, where Fo and Fc are the observed and calculated structure factor amplitudes, respectively.
c
Rfree was calculated with the 5% of reflections excluded from the overall data set.
d
The numbers in parentheses are results for the highest-resolution shell.