TABLE 1.
Data collection and refinement statistics for the KRIT1 FERM domain in complex with (i) Rap1b and (ii) Rap1b and the HEG1 cytoplasmic tail
| Rap1b (4hdo) | Rap1b and HEG1 (4hdq) | |
|---|---|---|
| Data collection | ||
| Space group | P21 | P21 |
| Cell dimensions | ||
| a, b, c | 57.9, 77.8, 58.9 Å | 57.3, 77.4, 58.6 Å |
| α, β, γ | 90.0, 91.2, 90.0° | 90.0, 95.6, 90.0° |
| Resolution | 50.0 to 1.67 Å (1.77 to 1.67 Å)a | 30 to 1.95 Å (2.07 to 1.95 Å)a |
| Rmerge | 4.6 (35.3) | 6.6 (34.7) |
| I/σI | 31.3 (4.4) | 21.0 (3.9) |
| Completeness | 96.0% (80.0%) | 99.1% (96.8%) |
| Redundancy | 3.6 (2.8) | 3.3 (2.9) |
| Refinement | ||
| Resolution | 32.4 to 1.67 Å | 29.2 to 1.95 Å |
| No. of reflections | 55,017 | 35,112 |
| Rwork/Rfree | 21.3/23.1 | 20.4/26.2 |
| No. of atoms | 4167 | 4014 |
| Protein | 3860 | 3883 |
| Ligand/ion | 39 | 39 |
| Water | 268 | 92 |
| B-factors | 23.4 | 38.0 |
| Protein | 23.0 | 38.1 |
| Ligand/ion | 20.4 | 34.7 |
| Water | 28.7 | 34.5 |
| Root mean square deviations | ||
| Bond lengths | 0.005 Å | 0.02 Å |
| Bond angles | 1.006° | 1.943° |
a The highest resolution shell is shown in parentheses.