Table 1.
Crystallographic data collection and refinement statistics.
| Data collection and processing | |
|---|---|
| Space group | P 41 21 2 |
| Cell dimensions | |
| a, b, c (Å) | 81.95, 81.95, 155.93 |
| α, β, γ (°) | 90, 90, 90 |
| Resolution rangea (Å) | 46.51−2.59 (2.72−2.59) |
| Ellipsoidal highest resolutionb (Å) / direction |
2.58 / a* 2.58 / b* 2.76 / c* |
| Number of unique reflectionsa | 15,457 (774) |
| Rsyma | 0.10 (3.69) |
| Rpima | 0.02 (0.70) |
| <I/σ(I)> a | 21.4 (1.1) |
| CC1/2a | 1.00 (0.66) |
| Completeness, sphericala (%) | 89.5 (33.3) |
| Completeness, ellipsoidala,b (%) | 94.9 (55.5) |
| Redundancya | 25.7 (28.1) |
| Structure refinement | |
| Resolution rangea (Å) | 43.89−2.59 (2.68−2.59) |
| Number of unique reflectionsa | 15,453 (321) |
| Rwork / Rfreea | 0.19 / 0.22 (0.36 / 0.39) |
| Number of atoms | |
| Protein | 2323 |
| Ligands/ions | 4 |
| Water | 303 |
| Average B-factor (Å2) | |
| Protein | 106 |
| Ligands/ions | 124 |
| Water | 93 |
| R.m.s. deviations | |
| Bond lengths (Å) | 0.003 |
| Bond angles (°) | 0.62 |
aValues in parentheses are for the highest-resolution shell.
bThe datasets were anisotropically truncated using the STARANISO web server. An ellipsoid was fitted to the anisotropic cut-off surface to provide approximate resolution limits along three directions in reciprocal space. The real cut-off surface is only approximately ellipsoidal and the directions of the worst and best resolution limits may not correspond with the reciprocal axes.