Table I. Crystallographic data and refinement statistics of SbHCT.
| Parameter | Apo-Form | Complex |
|---|---|---|
| Data | ||
| Beam line | ALS 8.2.1 | ALS 8.2.1 |
| Wavelength (Å) | 1.0 | 1.0 |
| Resolution (Å) | 50–2.0 | 50–2.4 |
| Space group | P65 | P65 |
| Cell dimensions (Å) | a = 135.9 | a = 137.2 |
| b = 135.9 | b = 137.2 | |
| c = 64.0 | c = 63.6 | |
| Asymmetric unit | 1 | 1 |
| Total observations | 491,611 | 465,320 |
| Unique reflections | 44,714 | 44,241 |
| Completeness (%) | 99.9 (94.0) | 97.0 (90.0) |
| Rsyma,b | 0.076 (0.627) | 0.086 (0.479) |
| Refinement | ||
| Resolution (Å) | 44.5–2.0 | 43.4–2.4 |
| No. of reflections | 43,938 | 25,964 |
| Rcrystc (%) | 18.3 | 20.4 |
| Rfreed (%) | 20.7 | 25.4 |
| r.m.s.d.e bonds (Å) | 0.007 | 0.008 |
| r.m.s.d.e angles (°) | 1.012 | 1.119 |
| No. of atoms | ||
| Protein and ligand | 3,409 | 3,421 |
| Water | 334 | 127 |
a
Numbers in parentheses refer to the highest shell. bRsym = Σ|Ih − < Ih>|/ΣIh, where < Ih> is the average intensity over symmetry equivalent reflections. cRcryst = Σ|Fobs − Fcalc|/Fobs, where summation is over the data used for refinement. dRfree was calculated as for Rcryst using 5% of the data that was excluded from refinement. eRoot mean square deviation.