Crystallographic data collection and refinement statistics
Statistic | |
|---|---|
| X-ray data collection | |
| Space group | P43212 |
| Cell dimensions | |
| a, b, c (Å) | 90.9, 90.9, 85.4 |
| α, β, γ (°) | 90.0, 90.0, 90.0 |
| Resolution (Å) (highest shell) | 50-2.8 (3.0-2.8)a |
| Rsym (%)b | 10.5 (43.5) |
| I/σ | 20 (2.8) |
| Completeness (%) | 99.7 (97.6) |
| Redundancy | 10 (6.3) |
| Crystallographic refinement | |
| Resolution (Å) | 50-2.8 (3.0-2.8) |
| Unique reflections | 8870 (1166) |
| Mean thermal displacement parameter (Å2) | |
| Protein | 48.1 |
| Water | 44.4 |
| RMSD | |
| Bond lengths (Å) | 0.008 |
| Bond angles (°) | 1.2 |
| Rwork/Rfree (%)c,d | 24.2 (34)/28.4 (38.7) |
↵ a Data for the outer shell are given in parentheses.
↵ b Rsym = (∑hkl∑i| Ii (hkl) - <I (hkl)>|)/∑hkl∑i Ii ((hkl)) for n independent reflections and observations of a given reflection, <I (hkl)> is the average intensity of the I observation.
↵ c Rwork = ∑||Fo| - |Fc||/∑|Fo|, where Fo is the observed amplitude of an X-ray reflection, and Fc is the calculated amplitude of this reflection derived fromn the refined coordinates.
↵ d Rfree is the R-factor calculated using 10% of randomly selected reflections.