TABLE 1.
X-ray diffraction data and refinement statisticsa
| Parameter (unit) | Soluble form | Refolded form |
|---|---|---|
| Wavelength (Å) | 0.9794 | 0.9794 |
| Resolution (Å) | 15-2.8 (2.87-2.80) | 15-3.23 (3.23-3.39) |
| Redundancy | 3.7 (3.4) | 4.6 (3.2) |
| Unique reflections | 90,937 (9,649) | 40,607 (4,066) |
| Completeness (%) | 96.6 (94) | 99.1 (99.5) |
| <I/σI> | 14.4 (1.7) | 19.3 (2.4) |
| Rsym (Σ|I − <I>|/ΣI) | 0.095 (0.489) | 0.053 (0.540) |
| Rcryst (Σ∥Fo| − |Fc∥/Σ|Fo|) | 0.21 (0.24) | 0.22 (0.30) |
| Rfree (5% of data) | 0.27 (0.29) | 0.25 (0.33) |
| No. of protein atoms/AUb | 10,395 | 3,358 |
| RMSD in bonds (Å) | 0.016 | 0.012 |
| RMSD angles (°) | 1.381 | 1.422 |
| Solvent molecules (no.) | 160 | 0 |
a
Values in parentheses are for the outermost resolution shell.
b
AU is an abbreviation for asymmetric unit.