Table 1. X-ray diffraction data collection and refinement statistics.
| SmSULT + R-OXA | SmSULT + S-OXA | |
|---|---|---|
| PDB code | 5BYJ | 5BYK |
| Data collection | ||
| Space group | P21212 | P21212 |
| Cell dimensions | ||
| a, b, c (Å) | 140.5, 39.2, 54.0 | 140.6, 39.4, 54.0 |
| α, β, γ (°) | 90, 90, 90 | 90, 90, 90 |
| Wavelength (Å) | 0.9792 | 0.9792 |
| Resolution (Å) | 42.82–1.80 (1.90–1.80)* | 54.00–1.28 (1.35–1.28) |
| R sym | 0.054 (0.652) | 0.052 (0.693) |
| R pim | 0.027 (0.359) | 0.028 (0.365) |
| I/σI | 15.3 (2.1) | 14.9 (2.1) |
| Completeness (%) | 98.7 (98.5) | 97.8 (96.7) |
| Redundancy | 4.3 (4.0) | 4.3 (4.2) |
| Wilson value | 29.1 | 16.7 |
| Refinement | ||
| Resolution (Å) | 42.82–1.80 | 50.41–1.28 |
| No. reflections | 27,971 | 76,328 |
| R work/ R free | 0.173/0.204 | 0.152 (0.171) |
| No. atoms | ||
| Protein | 2,105 | 2,100 |
| Ligand/ion | 47 (1 PAP, 1 OXA) † | 57 (1 PAP, 1 OXA, 1 DMA, 1 Na+) |
| Water | 217 | 334 |
| B-factors (Å2) | ||
| Protein | 31.5 | 21.6 |
| Ligand | 32.3 | 21.6 |
| Solvent | 39.5 | 35.8 |
| R.m.s deviations | ||
| Bond lengths (Å) | 0.007 | 0.007 |
| Bond angles (°) | 1.054 | 1.105 |
| Ramachandran statistics—favored, allowed, outliers (%) | 97.2, 2.8, 0.0 | 98.1, 1.9, 0.0 |
*Highest resolution shell is shown in parentheses.
†Ligand abbreviations: DMA—dimethylarsenic cysteine (cysteine modified by cacodylate present in the crystallization buffer), OXA—oxamniquine, PAP—adenosine-3'-5'-diphosphate