Table 1.
Crystallographic data collection and refinement
| xtFAM46B | |
|---|---|
| Data collection | |
| Space group | P 1211 |
| Cell dimensions | |
| a, b, c (Å) | 59.6, 76.1, 135.1 |
| α, β, γ (°) | 90, 96.5, 90 |
| Wavelength (Å) | 0.97915 |
| Resolution (Å)a | 47.1–2.69 (2.79–2.69) |
| No. reflections | 33266 (3214) |
| R sym | 0.083 (0.439) |
| I / σ(I) | 14.12 (3.65) |
| Completeness (%) | 99.2 (97.6) |
| Redundancy | 3.41 (3.36) |
| Refinement | |
| R work/Rfree | 0.204/0.252 |
| No. atoms | |
| Protein | 7988 |
| Ligand/ion | 39 |
| Water | 40 |
| B-factors | |
| Protein | 63.18 |
| Ligand/ion | 100.96 |
| Water | 44.02 |
| R.m.s. deviations | |
| Bond lengths (Å) | 0.002 |
| Bond angles (°) | 0.54 |
| Ramachandran | |
| Favored (%) | 96.5 |
| Outliers (%) | 0 |
aNumbers in parentheses represent values from the highest resolution shell.