Table 1.
Data collection, phasing and refinement statistics for the crystal structure
| SeMet RBBP510–325-RBBP5390–480d | |
|---|---|
| Data collection | |
| Space group | P1 |
| Cell dimensions | |
| a, b, c (Å) | 57.6, 68.8, 72.8 |
| α, β, γ (°) | 99.2, 99.3, 113.8 |
| Wavelength (Å) | 0.9785(Se peak) |
| Resolution (Å) | 50–1.8 |
| R merge | 0.08(0.42) * |
| I/σI | 20.0 (2.5) |
| Completeness (%) | 96.3 (89.2) |
| Redundancy | 6.7/5.5 |
| Refinement | |
| Resolution (Å) | 34.8–1.8 |
| No. reflections | 86 883 |
| R work /R free (%)b | 16.5/19.4 |
| No. atoms | |
| Protein | 5387 |
| Solvent & ligands | 576 |
| B-factors (Å2) | |
| Protein | 30.8 |
| Solvent & ligands | 45.4 |
| R.m.s. deviations | |
| Bond lengths (Å) | 0.008 |
| Bond angles (°) | 0.962 |
* Highest resolution shell is shown in parenthesis.