Table 2.
Crystallographic Data Statistics
| Complexa X-ray Source |
C13.28-GRK2-Gβ1γ2 APS 21-ID-G |
C13.18-GRK2 APS 21-ID-G |
|---|---|---|
| Wavelength (Å) | 0.97856 | 0.97856 |
| Dmin (Å) | 4.5 (4.58-4.50) | 3.5 (3.56-3.50) |
| Space Group | P312 | P21212 |
| Unit cell constants | a=257 Å | a=113.3 Å |
| b=257 Å | b=139.7 Å | |
| c=99.4 Å | c=60.9 Å | |
| α=β=90°; γ=120° | α=β=γ=90° | |
| No. crystals | 1 | 2 |
| Unique reflections | 12,758 (96) | 8,251 (92) |
| Average multiplicity | 3.9 (2.3) | 7.8 (8.3) |
| Rsym (%) | 6.4 (38.8) | 10.3 (49.0) |
| Completeness (%)b | 58.4 (9.0) | 65.5 (14.8) |
| <I>/<σI> | 24.5 (1.6)c | 28.9 (4.7) |
|
| ||
| Refinement resolution | 20.0-4.52 (4.63-4.52) | 25.0-3.51 (3.60-3.51) |
| Total reflections used | 11,919 (154) | 7,811 (87) |
| Protein atoms | 8,112 | 4,746 |
| Non-protein atoms | 401 | 168 |
| RMSD bond lengths (Å) | 0.005 | 0.005 |
| RMSD bond angles (°) | 0.86 | 0.91 |
| Est. coordinate error (Å) | 0.95 | 0.67 |
| Ramachandran most favored, disallowed (%) | 83.1, 0.0 | 84.7, 0.0 |
| Rwork (%) | 18.4 (26.8) | 21.6 (41.4) |
| Rfree (%) | 26.8 (37.1) | 31.7 (37.1) |
| PDB Entry | 3UZS | 3UZT |
a
These crystal forms represent the best diffracting crystals of the various aptamers in complex with GRK2 (see Table 1 and S1).
b
Data sets were elliptically truncated to the maximum resolution in each direction as described in the methods.
c
A I/σI cutoff of 0 was applied to this crystal form during scaling.