Table 1. Summary of the crystallographic analysis of the cytoplasmic domain of the Kir3.2 E236R mutant.
| Data collection | ||
|---|---|---|
| Space group | P4212 | |
| Cell dimensions | a, b, c (Å) | 85.86, 85.86, 73.05 |
| α, β, γ (°) | 90, 90, 90 | |
| Resolution (Å) | 50-2.0 (2.07-2.00) a | |
| R sym | 0.125 (0.801) a | |
| I/σI | 673.6 (26.4) a | |
| Completeness (%) | 99.7 (100) a | |
| Redundancy | 27.3 (27.2) a | |
| Refinement | ||
| Resolution (Å) | 30-2.0 | |
| No. reflections | 17,846 | |
| R work/R free | 21.6/26.0 | |
| No. atoms | Protein/Ligand (ions)/water | 1595/9/84 |
| B factors | Protein (main chain) | 41.7 |
| Protein (side chains)/ligands/ions/waters | 43.3/68.4/79.5/45.7 | |
| r.m.s.d. b | Bond lengths (Å) | 0.009 |
| Bond angles (°) | 1.06 | |
| Ramachandran analysis (%) | Core, allowed, generously allowed, disallowed | 88.6/11.4/0.0/0.0 |
a Values in parentheses are for the highest-resolution shell.
b r.m.s.d., root mean square deviation.