TABLE 1.
Crystallographic data collection and refinement statistics
| Statistic | |
|---|---|
| X-ray data collection | |
| Space group | P212121 |
| Cell dimensions | |
| a, b, c (Å) | 55.6, 179.9, 200.6 |
| α, β, γ (°) | 90.0, 90.0, 90.0 |
| Resolution (Å) (highest shell) | 48–3.1 (3.3–3.1)a |
| Rsym (%)b | 13.1 (48.1) |
| I/σ | 13.6 (4.5) |
| Completeness (%) | 97.5 (94.0) |
| Redundancy | 7.0 (6.2) |
| Crystallographic refinement | |
| Resolution (Å) | 48–3.1 (3.3–3.1) |
| Unique reflections | 36,488 |
| Mean thermal displacement parameter (Å2) | |
| Protein | 53.9 |
| Water | 49.2 |
| Root-mean-square deviation | |
| Bond lengths (Å) | 0.014 |
| Bond angles (°) | 1.70 |
| Rwork/Rfree (%)c,d | 26.6 (26.8)/29.9 (29.6) |
a
Number in parentheses is for the highest shell.
b
Rsym = Σ|I − 〈I〉|Σ I, where I is the observed intensity and 〈I〉 is the average intensity of multiple symmetry-related observations of that reflection.
c
Rwork = Σ ‖Fo| − |Fc‖/Σ|Fo|, where Fo and Fc are the observed and calculated structure factors, respectively.
d
Rfree = Σ ‖Fo| − |Fc‖/Σ|Fo| for 7% of the data not used at any stage of structural refinement.