TABLE 2.
Crystallographic statistics
Low completeness values reflect the fact that an elliptical mask was applied prior to scaling was used to accommodate highly anisotropic diffraction data (Lodowski et al., 2003). Without the mask, data had 82.4% overall completeness and 82% in the highest resolution shell for 4MK0 and 100% overall completeness and 100% completeness in the highest resolution shell for 4L9I.
| Protein Complex | GRK2·CCG-206584–Gβγ | GRK1·Paroxetine |
|---|---|---|
| X-ray source | LS-CAT ID-D | LS-CAT ID-G |
| Wavelength (Å) | 1.1272 | 1.0793 |
| Dmin(Å) | 19.99-2.4 (2.44-2.4) | 29.9-2.32 (2.36-2.32) |
| Space group | C2221 | P 212121 |
| Cell constants | a=61.2, b=240.9, c=212.0 | a=66. 8, b=122.1, c=152.9 |
| Unique reflections | 30794 | 54845 |
| Rsym (%) | 10.6 (39.0) | 10.9 (94.9) |
| Completeness (%) | 49.9 (1.0) | 36.9 (0.8) |
| I/σI | 61.7/4.0 (7.0/3.0) | 49.7/1.8 (5.4/2.0) |
| Redundancy | 5.0 (2.8) | 9.1 (9.2) |
| Refinement resolution (Å) | 20.0-2.4 (2.47-2.4) | 29.9-2.32 (2.38-2.32) |
| Total reflections used | 29,079 | 51,966 |
| RMSD bond lengths (Å) | 0.004 | 0.009 |
| RMSD bond angles (°) | 0.875 | 1.4 |
| Est. coordinate error (Å) | 0.409 | 0.30 |
| Ramachandran plot | ||
| Most favored, outliers (%) | 94.1, 0.1 | 96.7, 0.1 |
| Rwork | 19.5 (38.3) | 18.8 (24.5) |
| Rfree | 24.6 (81.1) | 22.9 (28.8) |
| Protein atoms | 8235 | 7894 |
| Water molecules | 147 | 309 |
| Inhibitor atoms | 25 | 48 |
| Average B-factor (Å2): | 55.3 | 23.4 |
| Protein | 55.9 | 19.4 |
| Inhibitor | 50 | 20.8 |
| MolProbity score | 1.28 (100th percentile) | 1.37 (100th percentile) |
| MolProbity Ramachandran outlier | 1 | 1 |
| MolProbity Cβ deviations | 0 | 0 |
| MolProbity bad backbone bonds | 0 | 0 |
| MolProbity bad backbone angles | 0 | 0 |
| PDB ID | 4MK0 | 4L9I |