Table 1. Data collection and refinement statistics.
| Data Collection | ||
|---|---|---|
| Protein | Acl428–361·RpL41-277 | hsKap104·RpL4308–332 |
| PDB ID | 5TQB | 5TQC |
| Synchrotron | SSRL* | SSRL* |
| Beamline | 12–2 | 12–2 |
| Space group | P21212 | P21212 |
| Cell dimensions | ||
| a, b, c (Å) | 121.0, 127.9, 42.7 | 68.6, 130.7, 174.2 |
| α, β, γ (°) | 90.0, 90.0, 90.0 | 90.0, 90.0, 90.0 |
| Se Peak | Native | |
| Wavelength (Å) | 0.9792 | 1.0000 |
| Resolution (Å) | 50.0–2.4 | 50.0–3.0 |
| Rmerge (%)† | 8.9 (99.0) | 9.3 (192.7) |
| Rpim (%)† | 2.6 (28.5) | 2.7 (53.5) |
| <I>/<σI>† | 13.6 (1.9) | 20.7 (1.6) |
| CC1/2 † | 99.9 (89.8) | 99.9 (75.7) |
| Completeness (%)† | 99.1 (99.1) | 99.8 (99.9) |
| No. of observations | 338,722 | 425,167 |
| No. of unique reflections† | 49,797 (8,039) | 32,119 (5,078) |
| Redundancy† | 6.8 (6.6) | 13.2 (13.7) |
| Refinement | ||
| Resolution (Å) | 50.0–2.4 | 50.0–3.0 |
| No. of reflections | 49,767 | 32,065 |
| No. of reflections test set | 2,505 (5.0%) | 1,606 (5.0%) |
| Rwork/Rfree (%) | 19.1/22.7 | 20.8/23.8 |
| No. atoms | 4,605 | 6,750 |
| Protein | 4,510 | 6,750 |
| Ligands | 39 | 0 |
| Water | 56 | 0 |
| B-factors | ||
| Protein | 73 | 103 |
| Ligands | 87 | N/A |
| Water | 60 | N/A |
| r.m.s.d. | ||
| Bond lengths (Å) | 0.004 | 0.002 |
| Bond angles (°) | 0.7 | 0.7 |
| Ramachandran plot‡ | ||
| Favored (%) | 96.7 | 97.4 |
| Outliers (%) | 0.0 | 0.0 |
| MolProbity | ||
| Clash score‡ | 1.98 | 1.77 |
| MolProbity score‡ | 1.17 | 1.05 |
Crystallographic analysis.
*SSRL, Stanford Synchrotron Radiation Lightsource.
†Highest-resolution shell is shown in parentheses.
‡As determined by MolProbity30.