Table 1.
X-ray phasing and refinement
| Compound 1 | Compound 2 | |
| X-ray diffraction data | ||
| Wave length (Å) | 0.9795 | 0.9796 |
| Resolution (Å) | 2.5 (2.59–2.50) | 2.8 (2.9–2.8) |
| Observations | 246,835 | 161,058 |
| Uniquea | 41,522 | 16,580 |
| Completeness (%) | 98 (97) | 99 (99) |
| I / σI | 13.3 (4.2) | 8.8 (3.4) |
| Rsym (%) | 5.0 (36) | 10.6 (50) |
| SAD Phasing (20–2.5 Å) | ||
| Se sites | 11 | |
| Z-Score (SOLVE) | 30.7 | |
| Figure of Merit (SOLVE) | 0.28 | |
| Figure of Merit (DM) | 0.73 | |
| Model refinement | ||
| Reflections (work/free) | 21,573/1166 | 15,665/851 |
| Completeness (work/free %) | 94.3/5.1 | 93.9/5.1 |
| Rfactor (work/free %) | 23.8/29.0 | 24.3/31.8 |
| Protein residues | 454 | 454 |
| Solvent molecules | 140 | 137 |
| Mean B factor(Å2) | 53 | 54 |
| RMSD ideal bond lengths (Å) | 0.008 | 0.007 |
| RMSD ideal bond angles (°) | 1.30 | 1.33 |
| RMSD ideal dihedral (°) | 22.8 | 22.8 |
| RMSD ideal improper (°) | 0.78 | 0.74 |
a Bijvoet pairs separated Rsym =∑|I-〈I〉|∑I, where I is the integrated intensity for a reflection. Figure of Merit = 〈∑P(α)eiα/∑P(α)〉, where P(α) is the phase probability at angle α. Rfactor = ∑|FP-FC|/∑FP,where FP and FC are the observed and calculated structure factor amplitudes, while Rfree. is calculated on 5% of the data excluded from refinement. Values in parentheses are for the highest resolution shell.