Table 1.
Data collection and refinement statistics for KCTD5 crystals
| High-salt KCTD5 Se-Met PDBid 3DRX | Low-salt KCTD5 Native PDBid 3DRY | N-terminal domain PDBid 3DRZ | |
|---|---|---|---|
| Data collection | |||
| Space group | P 21 21 21 | P 21 21 21 | P 21 21 21 |
| Cell dimensions | |||
| a, b, c (Å) | 72.9, 128.6, 152.5 | 103.0, 106.8, 110.1 | 59.03, 90.72, 110.16 |
| α,β,γ (°) | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 |
| Resolutionb) (Å) | 20–3.1 (3.2–3.1) | 20–3.3 (3.4–3.3) | 20–1.9 (1.95–1.90) |
| Rmerge* | 0.072 (0.46) | 0.089(0.56) | 0.065 (0.45) |
| I/σ* | 12.4 (2.3) | 11.3 (2.0) | 15.4 (2.5) |
| Completeness (%)* | 98.9 (93.8) | 99.7 (98.5) | 99.7 (98.4) |
| Redundancy* | 4.4 (4.5) | 4.3 (4.4) | 4.5 (4.5) |
| Refinement | |||
| Resolution (Å) | 20–3.1 | 20–3.3 | 20–1.9 |
| No. reflections | 25,986 | 18,687 | 46,924 |
| Rwork/Rfree | 0.227/0.275 | 0.252/0.308 | 0.193/0.232 |
| No. atoms | |||
| Protein | 6915 | 6815 | 4095 |
| Water | - | - | 359 |
| B-factors | |||
| Protein | 67 | 73 | 35.1 |
| Water | - | - | 42.0 |
| R.m.s deviations | |||
| Bond lengths (Å) | 0.008 | 0.012 | 0.009 |
| Bond angles (°) | 1.05 | 1.28 | 1.196 |
Legend: One crystal was used for each data collection. Asterisks (*) indicate where data in parentheses correspond to last resolution shell.