Table 1.
Crystallographic data collection and refinement statistics
| Data Collection | |
|---|---|
| Beamline | ALS 8.3.1 |
| Wavelength (Å) | 1.11 |
| Space group | P 21 21 21 |
| Cell dimensions | |
| a, b, c (Å) | 48.1, 78.0, 106.2 |
| α, β, γ (°) | 90.0, 90.0, 90.0 |
| Resolution (Å) | 63 – 2.4 (2.45 – 2.4)a |
| Rmergeb (%) | 10.3 (89.0) |
| <I>/<σ>c | 10.8 (1.1) |
| Completeness (%) | 98.8 (98.5) |
| Refinement | |
| No. of reflections | 16,260 |
| Rworkc (%) | 21.5 |
| Rfreed (%) | 24.7 |
| No. of atoms | |
| Protein | 2441 |
| Ligand/ion | 32 |
| Water | 11 |
| RMSD | |
| Bond lengths (Å) | 0.002 |
| Bond angle (°) | 0.45 |
| Ramachandran plot (%) | |
| Favored | 97.0 |
| Allowed | 3.0 |
| Outliers | 0.0 |
a
Values in parentheses are for the highest resolution shell.
b
Rmerge= Σhkl Σj | I j − 〈 I 〉 |/Σhkl ΣIj, where j is the jth measurement and <I> is the weighted mean of I.
c
<I>/<σ> is the mean intensity divided by the mean error.
d
Rwork= Σhkl || Fo | − k | Fc ||/Σhkl | Fo |, where Fo and Fc are the observed and calculated structure factor amplitudes, and k is a weighting factor.
e
Rfree is the same as Rwork calculated on 5% of the reflections.