Table 1. Structural features of AcrIIA22.
| Data collection | |
| Space Group | P4332 |
| Cell Dimensions | |
| a, b, c (Å) | 128.56, 128.56, 128.56 |
| α, β, γ (°) | 90.0, 90.0, 90.0 |
| Resolution (Å) | 50.00–2.80 |
| Rmerge | 0.106 (0.906) |
| I/σI | 17.4 (2.6) |
| Completeness (%) | 98.7 (100.0) |
| Redundancy | 10.4 (10.7) |
| CC 1/2 | 0.837 |
| Refinement | |
| No. Reflections | 9,334 |
| Rwork (Rfree) (%) | 22.2 (24.6) |
| No. Complex in ASU | 2 |
| No. atoms | |
| Protein | 810 |
| Heteroatoms | 50 |
| Water | 3 |
| B-factor | 82.82 |
| R.m.s deviations | |
| Bond lengths (Å) | 0.003 |
| Bond angles (°) | 0.610 |
| Ramachandran | |
| Preferred (%) | 98.15 |
| Allowed (%) | 1.85 |
| Outliers (%) | 0 |