Table 1. Data collection and refinement statistics.
| SART3 HAT repeat domain | SART3 HAT-C-USP4 DUSP-UBL | SART3 NLS-ImpA | ||
|---|---|---|---|---|
| Native | Se-Met peak | |||
| Data collection | ||||
| Space group | P21 | P21 | P43212 | P212121 |
| Cell dimensions | ||||
| a, b, c (Å) | 120.9, 80.5, 146.6 | 123.8, 81.0, 146.9 | 114.3, 114.3, 303.6 | 114.3, 114.3, 303.6 |
| α, β, γ (°) | 90.0, 99.3, 90.0 | 90.0, 100.1, 90.0 | 90.0, 90.0, 90.0 | 90.0, 90.0, 90.0 |
| Resolution (Å) | 50.0–2.6 (2.69–2.60)a | 50.0–3.0 (3.11–3.00) | 50.0–3.0 (3.08–3.00) | 50.0–1.70 (1.76–1.70) |
| R sym or Rmerge | 9.7 (39.5) | 12.0 (33.1) | 10.7 (35.6) | 7.8 (45.3) |
| I / σI | 14.5 (2.1) | 12.1 (2.3) | 11.7 (2.1) | 19.8 (1.9) |
| Completeness (%) | 95.1 (82.9) | 97.3 (92.3) | 98.1 (97.0) | 99.0 (97.4) |
| Redundancy | 2.5 (1.6) | 4.0 (2.1) | 2.8 (2.0) | |
| Refinement | ||||
| Resolution (Å) | 50.0–2.6 | 50.0–3.0 | 50.0–1.7 | |
| No. reflections | 82 307 | 40 978 | 76 791 | |
| R work / Rfree | 23.5 / 28.1 | 30.9 / 33.4 | 19.1 / 21.9 | |
| No. atoms | ||||
| Protein | 16 629 | 8535 | 3385 | |
| Ligand/ion | 0 | 0 | 0 | |
| Water | 318 | 57 | 501 | |
| B-factors | ||||
| Protein | 44.3 | 54.9 | 19.3 | |
| Ligand/ion | 0 | 0 | 0 | |
| Water | 54.3 | 31.2 | 37.6 | |
| R.m.s. deviations | ||||
| Bond lengths (Å) | 0.008 | 0.005 | 0.017 | |
| Bond angles (°) | 1.45 | 0.98 | 1.58 | |
| MolProbity Scoreb | 1.90 | 2.98 | 1.54 | |
All diffraction data were obtained from a single crystal.
aValues in parentheses are for highest-resolution shell.
bMolProbity score combines the clashcore, rotamer and Ramachandran evaluations into a single score, normalized to be on the same scale as X-ray resolution.