Table 3.
Data collection statistics
| Ligand complex
|
BMS270394
|
BMS270395
|
|
|---|---|---|---|
| X-ray source | BW7B, DESY | ID13, ESRF Microfocus | BM14, ESRF |
| Wavelength, Å | 0.8345 | 0.6887 | 0.9612 |
| Approximated crystal size, μm3 | 560 × 280 × 280 | 100 × 60 × 80 | 200 × 120 × 120 |
| Cell, Å (α = β = γ = 90°) | a = b = 59.67 | a = b = 59.90 | a = b = 59.85 |
| Space group P41212 | c = 155.55 | c = 154.52 | c = 155.62 |
| Resolution, Å | 15–1.59 | 30–2.04 | 25–1.67 |
| Observed reflections | 131,831 | 46,012 | 165,142 |
| Unique reflections | 37,688 | 17,279 | 33,233 |
| Multiplicity | 3.50 | 2.66 | 4.97 |
| Completeness, % | 97.2 (91.2) | 92.8 (94.9) | 98.2 (97.9) |
| Rsym (I), % | 4.4 (30.8) | 6.9 (38.3) | 3.8 (31.5) |
| I/σ (I) | 27.0 (3.0) | 13.5 (2.9) | 33.1 (3.5) |
| Highest resolution shell, Å | 1.62–1.59 | 2.09–2.04 | 1.70–1.67 |
Refinement statistics for both enantiomer complexes performed with cns (17). Because the fluorine atom of BMS270395 was seen in two conformations, final occupancy refinement of the ligand was achieved with shelxl (20). Double conformations were observed essentially for residue side chains at the protein surface. Rcryst = Σhkl | Fobs − Fcalc |/Σhkl | Fobs |. Rfree = Σhklɛ T | Fobs − Fcalc |/Σhklɛ T | Fobs |, the test set T includes 5% of the data (29).