TABLE 2.
Data collection and refinement statistics (molecular replacement)
| Parametera | Value for the parameter in:b
|
|
|---|---|---|
| MuV-HN–GM2 complex | MuV-HN–SLeX complex | |
| Data collection | ||
| Space group | P61 | P61 |
| Cell dimensions | ||
| a, b, c (Å) | 137.26, 137.26, 178.01 | 137.42, 137.42, 177.81 |
| α, β, γ (°) | 90.00, 90.00, 120.00 | 90.00, 90.00, 120.00 |
| Resolution (Å) | 50–2.05 (2.09–2.05) | 50–2.5 (2.54–2.50) |
| Rsym | 0.111 (>1.00) | 0.20 (>1.00) |
| Rpim | 0.028 (0.376) | 0.05 (0.451) |
| CC1/2 | 0.999 (0.581) | 0.998 (0.609) |
| I/σI | 29.4 (1.56) | 19 (2.0) |
| Completeness (%) | 99.8 (97.1) | 100.0 (100.0) |
| Redundancy | 21.1 (7.6) | 20.8 (9.7) |
| Refinement | ||
| Resolution (Å) | 44.93–2.05 | 49.45–2.50 |
| No. of reflections | 118,595 | 65,599 |
| Rwork/Rfree | 18.3/20.1 | 17.4/20.5 |
| No. of atoms | ||
| Protein | 7,060 | 7,060 |
| Ligand/ion | 292 | 312 |
| Water | 467 | 470 |
| B factors (Å2) | ||
| Protein | 47.7 | 37.6 |
| Ligand/ion | 68.4 | 67.8 |
| Water | 50.1 | 40.2 |
| RMSD | ||
| Bond lengths (Å) | 0.003 | 0.003 |
| Bond angles (°) | 0.796 | 0.681 |
| Sugars in the minimal-energy conformation (%) | 90.0 | 90.9 |
a
CC1/2, Pearson correlation coefficient between two random half data sets; RMSD, root mean square deviation.
b
Single-crystal X-ray diffraction data were collected for each structure. Values in parentheses are for the highest-resolution shell.