TABLE 1.
Data collection and refinement statistics
Values in parentheses are for the outer resolution shell.
| NpAS-turanose | DgAS | DgAS-turanose | |
|---|---|---|---|
| Data collection | |||
| Space group | P21212 | C2221 | C2221 |
| a, b, c (Å) | 96.0, 116.3, 60.5 | 105.3, 110.2, 115.5 | 104.7, 110.4, 115.3 |
| α, β, γ (°) | 90.0, 90.0, 90.0 | 90.0, 90.0, 90.0 | 90.0, 90.0, 90.0 |
| Resolution (Å) | 29.27-1.85 (1.95-1.85)* | 33.38-1.97 (2.08-1.97) | 63.45-2.10 (2.21-2.10) |
| Rsym | 0.096 (0.332) | 0.086 (0.376) | 0.099 (0.324) |
| I/σI | 6.5 (2.2) | 8.3 (2.0) | 4.9 (2.1) |
| Completeness (%) | 99.6 (100) | 99.6 (99.8) | 100 (98.9) |
| Redundancy | 3.6 (3.6) | 4.0 (3.9) | 6.3 (4.2) |
| No. of molecule/AU | 1 | 1 | 1 |
| Matthews coefficient (Å3/Da) | 2.4 | 2.3 | 2.3 |
| Refinement | |||
| Resolution (Å) | 29.10-1.85 | 33.22-1.97 | 13-2.10 |
| No. of unique reflections | 58,309 (8,452) | 47,355 (6,837) | 39,319 (5,648) |
| Rwork/Rfree (%) | 14.7/18.6 | 14.4/18.7 | 14.6/20.7 |
| Total number of atoms | 5,867 | 5,956 | 5,712 |
| Number of residues in the protein | 632 | 651 | 651 |
| Number of ligand molecules | 2 Turanoses, 1 PEG | 1 Tris, 13 glycerols | 1 Turanose |
| Number of water molecules | 767 | 602 | 394 |
| B-factors (Å2) | |||
| Protein | 11.6 | 17.9 | 20.7 |
| Ligand | 19.9 | 36.9 | 26.4 |
| Water | 21.2 | 27.5 | 26.1 |
| R.m.s deviations | |||
| Bond lengths (Å) | 0.022 | 0.024 | 0.023 |
| Bond angles (°) | 1.8 | 1.8 | 1.9 |