TABLE 1.
Crystallographic data collection, reduction, and refinement statistics
| Type of measurement | Value |
|---|---|
| Collection | |
| Cell dimensions (Å) | a = 58.612, b = 80.410, c = 90.940 |
| Cell dimensions (°) | α = 68.681, β = 89.638, γ = 80.817 |
| Space group | P1 |
| Resolution (Å) | 30-2.3 (2.36-2.30)a |
| Wavelength (Å) | 1.1 |
| Distance (mm) | 140 |
| Mosaicity | 0.27 |
| Unique reflections | 61,284 |
| Multiplicity | 2.4 |
| I/σ | 7.3 (1.6) |
| Rmerge (%)b | 6.3 (40.6) |
| Completeness (%) | 96.2 |
| Refinement | |
| R factor (%)c | 19.74 |
| Rfree factor (%)c | 25.13 |
| No. of protein atoms | 10,772 |
| No. of water molecules | 256 |
| Ramachandran plot | |
| Core | 94.1% |
| Allowed | 5.6% |
| Generally allowed | 0.3% |
| Disallowed | 0.1% |
| RMS deviations | |
| Bond lengths (Å) | 0.012 |
| Bond angles (°) | 1.290 |
a
Values in parentheses are from the highest resolution shell.
b
Rmerge = Σ|I − <I>|/ΣI, where I is the integrated intensity of a given reflection.
c
R = Σ||Fobs| − |Fcalc||/Σ|Fobs |. Rfree was calculated using 5% of data excluded from refinement.