Table 1.
Data collection and refinement statistics for the NHERF1 PDZ2-CFTR complex
| Data collection | |
| Space group | I212121 |
| Cell dimensions | |
| a, b, c (Å) | 84.9, 85.0, 89.6 |
| α, β, γ (°) | 90.0, 90.0, 90.0 |
| Resolution (Å) | 19.8–2.20 (2.28–2.20) |
| Rmerge (%) | 17.6 (95.1) |
| Rpim (%) | 11.3 (60.0) |
| CC1/2 | 0.984 (0.634) |
| I/σ(I) | 4.3 (1.6) |
| Unique reflections | 16,795 (1653) |
| Completeness (%) | 99.6 (97.8) |
| Multiplicity | 3.5 (3.6) |
| Refinement | |
| Resolution (Å) | 19.8–2.20 (2.35–2.20) |
| No. of reflections: working/test | 16,735/783 (2566/124) |
| Rwork /Rfree | 20.6/23.3 (28.6/32.1) |
| No. of atoms | 2,138 |
| Protein | 1,934 |
| Water | 204 |
| Average B-factor (Å2) | 39.3 |
| Protein (Å2) | 40.0 |
| Water (Å2) | 32.9 |
| RMSD | |
| Bond lengths (Å) | 0.004 |
| Bond angles (Å) | 0.913 |
| Ramachandran | |
| Favored (%) | 98.0 |
| Allowed (%) | 2.0 |
| Disallowed (%) | 0.0 |