Table 1.
X-Ray data collection and refinement statistics
| MtNup188N (1–1160) | MtNup188N (1–1160) | MtNup188C (1445–1827) | |
|---|---|---|---|
| PDB code | 4KF7 | 4KF8 | |
| Data collection | |||
| Data set | Native | Selenomethionine | Selenomethionine |
| Space group | C2 | C2 | P212121 |
| a, b, c (Å) | 169.0, 94.8, 91.6 | 168.3, 94.6, 91.4 | 64.4, 66.7, 162.5 |
| α, β, γ (°) | 90, 98.9, 90 | 90, 98.4, 90 | 90, 90, 90 |
| Wavelength (Å) | 0.9792 | 0.9792 | 0.9792 |
| Resolution range (Å) | 66.8–2.65 (2.72–2.65) | 90.4–2.90 (3.02–2.90) | 81.1–3.00 (3.11–3.00) |
| Total reflections | 170,859 | 209,695 | 50,886 |
| Unique reflections | 41,673 | 58,249 | 14,539 |
| Completeness (%) | 100 (99.9) | 99.9 (98.8) | 99.9 (99.7) |
| Redundancy | 4.1 (3.8) | 3.6 (3.1) | 3.5 (3.1) |
| Rmerge(%) | 3.1 (77.2) | 3.0 (32.8) | 2.7 (56.1) |
| Rp.i.m.(%) | 2.0 (51.0) | 4.1 (26.3) | 1.6 (27.0) |
| I /σ(I) | 31.3 (1.8) | 9.6 (1.2) | 21.4 (4.8) |
| Wilson B factor (Å2) | 51.6 | 50.0 | 75.0 |
| Refinement | |||
| Resolution range (Å) | 66.8–2.65 | 81.1–3.00 | |
| Rwork (%) | 18.1 | 27.5 | |
| Rfree (%) | 22.5 | 29.4 | |
| Number of reflections | |||
| Total | 41,661 | 14,536 | |
| Rfree reflections | 1919 | 1139 | |
| Number of atoms | |||
| Protein | 8516 | 4366 | |
| Water | 128 | 0 | |
| B factors (Å2) | |||
| Protein | 64.4 | 92.3 | |
| Water | 44.9 | ||
| RMSD | |||
| Bond length (Å) | 0.004 | 0.003 | |
| Bond angles (°) | 0.904 | 0.769 | |
| Ramachandran plot | |||
| Favored (%) | 95.0 | 92.2 | |
| Allowed (%) | 4.1 | 6.8 | |
| Outliers (%) | 0.9 | 1.0 | |
The highest resolution shell is in parenthesis. Rmerge is the merging R factor. Rp.i.m. is the precision-indicating merging R factor. For definitions, see Weiss (2001).