Table 1.
X-ray data collection and refinement statistics
| Space group | C2221 |
| Unit cell dimensions (Å) | 104.9, 108.9, 143.2 |
| Maximum resolution (Å) | 2.4 |
| Completeness (%) | 83 (33) |
| I/σ(I) (overall) | 9.0 (1.8) |
| Rsym (%) | 7.1 (18.3) |
| Refinement resolution (Å) | 13.0–2.4 |
| Reflections | 26762 |
| Monomers/asymmetric unit | 2 |
| Protein atoms | 4712 |
| Solvent atoms (water) | 59 |
| Ligand atoms (biotin) | 32 |
| R (%) | 18.9 |
| Δbonds (Å) | 0.018 |
| Δangles (°) | 2.8 |
Rsym gives the agreement between repeated measurements of equivalent reflections. R is the crystallographic R-factor for the refined model. Rfree was not calculated because it would be susceptible to bias due to the noncrystallographic symmetry. Values given in parentheses correspond to the highest-resolution shell of data.