Table 1.
Data collection and refinement statistics
| Data collection | |
| Highest resolution, Å | 2.20 |
| Observed reflections | 52,353 |
| Unique reflections | 11,157 |
| Completeness, % | 96.9 |
| Rmerge* | 0.058 |
| Refinement | |
| Resolution, Å | 20.0–2.20 |
| Protein nonhydrogen atoms | 1,809 |
| Water molecules | 184 |
| Rcryst† | 0.211 |
| Rfree† | 0.288 |
| Average B-factor, Å2 | 36.2 |
| rmsd from ideal geometry | |
| Bond length, Å | 0.009 |
| Bond angles, ° | 1.1 |
| Torsion angles, ° | 20.8 |
*
Rmerge = ΣΣj|Ij(hkl) − 〈I(hkl)〉 |/Σ| 〈I(hkl)〉|, where Ij is the intensity measurement for reflection j and 〈I〉 is the mean intensity over j reflections.
†
Rcryst (Rfree) = Σ∥Fobs(hkl)| − |Fcalc(hkl)∥/Σ|Fobs(hkl)|, where Fobs and Fcalc are observed and calculated structure factors, respectively. Statistics are given for F > 2σ. Ten percent of the reflections were excluded from refinement and used to calculate Rfree.