TABLE 2 .
Crystallographic and refinement statistics
| Parameter | FdeC |
|---|---|
| Protein | |
| Space group | P21212 |
| No. of molecules in ASUd | 1 |
| Unit cell (Å) | 44.6, 150.93, 47.40 |
| Wavelength (Å) | 0.9202 |
| Resolution (Å) | 50.0-1.9 |
| Total no. of unique reflections | 24,734 |
| Completeness, % (highest shell) | 95.6 (67.0) |
| R merge, % (highest shell) | 0.084 (0.634) |
| Highest-resolution shell, Å | 1.97–1.90 |
| Mean I/σ (I) (highest shell) | 23.9 (1.7) |
| Refinement | |
| No. of references, working set | 23,413 |
| No. of references, test set | 1,265 |
| Rcryst (Rfreea)b (%) | 17.1 (20.5) |
| RMSD bonds (Å) | 0.017 |
| RMSD angles (°) | 1.44 |
| Avg B (Å)2 | 26.27 |
| ESUe based on Rfree (Å)c | 0.135 |
a
Rfree = as for Rcryst, but for 5.0% of the total reflections chosen at random and omitted from refinement.
b
R factor = Σ|Ii − <Ii>| |/Σ|Ii|, where Ii is the scaled intensity of the ith measurement and <Ii> is the mean intensity for that reflection.
c
Estimated overall coordinate error.
d
ASU, asymmetric unit.
e
ESU, estimated standard uncertainty.