Table 1.
X-ray crystallography data collection and structure refinement statistics
| Data collection | |
|---|---|
| Space group | P21 2 21 |
| Resolution (Å) | 29.61–2.84 (2.94–2.84) |
| Cell dimensions | |
| a, b, c (Å) | 74.15, 100.58, 236.59 |
| α, β, γ (°) | 90, 90, 90 |
| Rmerge (%) | 10.0 (128.2) |
| I/σI | 13.90 (1.40) |
| CC1/2 | 0.999 (0.60) |
| Completeness (%) | 99.6 (96.5) |
| Redundancy | 6.8 (6.8) |
| Refinement | |
|---|---|
| No. reflections | 42, 532 (4057) |
| Rwork/Rfree (%) | 18.6/25.2 |
| R.M.S deviations | |
| Bond angles (°) | 1.180 |
| Bond length (Å) | 0.009 |
| Average B-factor, all atoms (Å2) | 100.0 |
| Ramachandran plot of protein residues | |
| Preferred regions (%) | 95.97 |
| Allowed regions (%) | 4.03 |
| Number of residues | |
| RNA | 92 |
| Protein | 876 |
| Solvent | 180 |
Values in the parentheses are for the highest resolution shell