Table 1.
Data collection and refinement statistics
| PHF20 Tudor1a | PHF20 Tudor2a | |
|---|---|---|
| Data collection | ||
| Space group | P21 | P43 |
| Cell dimensions | ||
| a, b, c (Å) | 37.75, 60.76, 37.75 | 48.55, 48.55, 96.15 |
| α, β, γ (°) | 90.00, 112.82, 90.00 | 90.00, 90.00, 90.00 |
| Resolution (Å) | 30.38–1.93 (1.96–1.93)b | 23.54–2.00 (2.07–2.00) |
| Rmerge | 0.050 (0.370) | 0.058 (0.315) |
| I / σI | 16.3 (7.2) | 31.8 (3.6) |
| Completeness (%) | 98.1 (95.9) | 99.3 (95.6) |
| Redundancy | 7.1 (7.0) | 8.1 (6.8) |
| Refinement | ||
| Resolution (Å) | 30.38–1.93 (2.12–1.93) | 23.54–2.00 (2.15–2.00) |
| No. reflections | 11,693 (2,729) | 14,859 (2,900) |
| Rwork / Rfree | 0.229 / 0.236 | 0.235 / 0.262 |
| No. atoms | ||
| Protein | 2,327 | 888 |
| Water | 215 | 157 |
| B-factors | ||
| Protein | 33.4 | 53.9 |
| Water | 37.2 | 60.1 |
| R.m.s. deviations | ||
| Bond lengths (Å) | 0.005 | 0.003 |
| Ramachandran plot | ||
| Favored region (%) | 96.4 | 96.2 |
| Allowed region (%) | 3.6 | 1.9 |
a
A single crystal was used for each structure.
b
Values in parentheses are for highest- resolution shell.