Table 1. Data-collection and refinement statistics.
The P4322 crystal structure contains two independent IC5-4D molecules in the asymmetric unit. Values in parentheses are for the highest resolution shell.
| Data processing | |||
| Space group | P4322 | R3 | P21 |
| Unit-cell parameters | |||
| a (Å) | 96.07 | 228.56 | 76.59 |
| b (Å) | 96.07 | 228.56 | 46.91 |
| c (Å) | 321.92 | 69.98 | 95.79 |
| α (°) | 90 | 90 | 900 |
| β (°) | 90 | 90 | 104.3 |
| γ (°) | 90 | 120 | 90 |
| Wavelength (Å) | 0.97914 | 0.97914 | 0.97934 |
| Resolution (Å) | 25–3.7 (3.90–3.70) | 25–3.7 (3.90–3.70) | 25–2.5 (2.64–2.50) |
| Unique reflections | 16927 | 14474 | 23146 |
| R sym or R merge (%) | 13.1 (38.0) | 7.9 (79.6) | 6.3 (34.3) |
| 〈I/σ(I)〉 | 5.2 (2.0) | 7.7 (1.0) | 7.7 (2.2) |
| Completeness (%) | 99.6 (99.6) | 99.9 (100) | 99.7 (100) |
| Multiplicity | 7.4 (7.8) | 5.8 (5.8) | 3.7 (3.8) |
| Refinement | |||
| Resolution (Å) | 25–3.7 | 25–3.7 | 25–2.5 |
| No. of reflections | 16867 | 11463 | 23137 |
| R work/R free (%) | 23.0/28.0 | 22.9/27.3 | 23.9/26.6 |
| No. of atoms | |||
| Protein | 5704 | 2827 | 2912 |
| Carbohydrates | 397 | 284 | 204 |
| Ligands | 4 | 124 | |
| Water | 94 | ||
| Average B factors (Å2) | |||
| Protein | 140 | 185 | 84 |
| Carbohydrates | 181 | 268 | 112 |
| Ligands | 94 | 44 | |
| Water | 57 | ||
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.003 | 0.005 | 0.004 |
| Bond angles (°) | 0.734 | 1.105 | 0.967 |