Table 1.
Crystallographic data and refinement statistics
| Data statistics | |
| Resolution, Å | 20.0–2.08 |
| Unique reflections | 3,740 |
| Multiplicity | 2.8 |
| Completeness | 87.2% (80.7%) |
| Rsym* | 3.5% (11.0%) |
| I/3σ | 83.9% (65.0%) |
| Refinement statistics | |
| Rcryst† | 18.0% |
| Rfree† | 28.0% |
| rmsbond | 0.034 Å |
| rmsangle | 3.10° |
| Protein atoms | 610 |
| Water molecules | 60 |
*
Rsym = ∑hkl/∑j|Ij,hkl − 〈Ihkl|/∑hkl∑jIj,hkl, where 〈Ihkl〉 is the average of the intensity Ij,hkl over j = 1, … , N observations of symmetry equivalent reflections hkl.
† Rcryst = (∑ ∥ Fo| − |Fc ∥)|/∑|Fo|, where |Fo| and |Fc| are the observed and scaled calculated structure factor amplitudes, respectively.
Rfree is the R factor with 10% of the data that were excluded from refinement.