Table 1. Data collection and structural refinement of the rEglA crystals.
The statistics were calculated using the programs HKL-2000, REFMAC5 and Coot. Values in parentheses are for the highest resolution shells.
| Unliganded rEglA | E154A–cellotriose | |
|---|---|---|
| Data collection | ||
| Space group | P6122 | P6122 |
| Unit-cell parameters (Å, °) | a = b = 83.4, c = 225.1, α = β = 90, γ = 120 | a = b = 82.2, c = 221.8, α = β = 90, γ = 120 |
| Resolution range (Å) | 30–2.0 (2.03–2.00) | 30–2.2 (2.24–2.20) |
| Unique reflections | 31439 (1530) | 22798 (1110) |
| Multiplicity | 39.5 (42.8) | 23.1 (25.0) |
| Completeness (%) | 97.9 (97.1) | 97.0 (97.3) |
| Average I/σ(I) | 54.6 (8.8) | 60.7 (8.3) |
| Rmerge (%) | 7.5 (43.7) | 7.6 (61.9) |
| Refinement | ||
| Resolution range (Å) | 30–2.0 (2.05–2.00) | 30–2.2 (2.26–2.20) |
| Positive reflections | 29845 (2240) | 21543 (1629) |
| Rwork (%) | 17.0 (16.4) | 16.3 (18.9) |
| Rfree (%) | 21.6 (22.9) | 21.9 (27.5) |
| R.m.s.d. bond lengths (Å) | 0.020 | 0.018 |
| R.m.s.d. bond angles (°) | 2.1 | 1.9 |
| Dihedral angles in | ||
| Preferred regions (%) | 93.4 | 92.4 |
| Allowed regions (%) | 5.5 | 6.8 |
| Other regions (%) | 1.1 | 0.8 |
| No. of non-H atoms | ||
| Protein | 2971 | 2890 |
| Solvent | 231 | 180 |
| Ligand | 4 | |
| Average B (Å2) | ||
| Protein | 40.3 | 38.3 |
| Solvent | 49.5 | 47.4 |
| Ligand | 34.5 | |