Table 2 Data collection and refinement statistics.
From: Ligand-induced conformational changes in a thermophilic ribose-binding protein
| Â | tmRBP-apo | tmRBP-ribose |
|---|---|---|
Data Collection | Â | Â |
   Wavelength (Å) | 0.997 | 0.979 |
   Resolution (Å) | 1.40 | 2.15 |
   Unique reflections | 115460 | 25783 |
   Mean I/σ(I)a | 34.2 (1.7) | 25.7 (3.6) |
   Completeness (%)a | 99.0 (88.8) | 80.9 (21.0) |
   Rsym (%)a | 5.0 (51.5) | 5.6 (28.4) |
   Redundancya | 5.8 (3.4) | 5.8 (1.6) |
Refinement | Â | Â |
   Resolution (Å) | 50.0–1.40 | 50.0–2.15 |
   Num. of Reflections (working set/test set) | 115460/5767 | 23715/1354 |
   Rcryst (%) | 18.0 (28.0) | 19.3 (25.4) |
   Rfree b (%) | 20.3 (32.9) | 22.3 (29.2) |
   Number of atoms |  |  |
Protein | 4326 | 2286 |
Water | 627 | 142 |
Ligand | 0 | 10 |
r.m.s.d. | Â | Â |
   Bond lengths (Å) | 0.009 | 0.012 |
   Bond angles (°) | 1.2 | 1.2 |
Average B-factor (Ã… 2 ) | Â | Â |
   Main Chain | 15.3 | 34.5 |
   Side Chain | 17.3 | 35.8 |
   Solvent | 29 | 37.7 |
   Ligand |  | 24.8 |
Protein Geometry | Â | Â |
   Ramachandran outliers (%) | 0.4 | 0.3 |
   Ramachandran favored (%) | 98.7 | 97.6 |
   Rotamer outliers (%) | 2.2 | 3.0 |