Table I.
Data collection and refinement statistics
| Data set | Nup107 658–925 Nup133 934–1156 | Nup107 658–925dF Nup133 934–1156 | SeMet |
|---|---|---|---|
| Data collection | |||
| Wavelength | 0.9792 | 0.9792 | 0.9792 |
| Space group | C2 | P212121 | C2 |
| Cell dimensions | |||
| a, b, c (Å) | 51.7, 127.9, 152.7 | 47.6, 65.5, 193.2 | 51.9, 128.8, 153.4 |
| abg(°) | 90.0, 97.36, 90.0 | 90.0, 90.0, 90.0 | 90.0, 97.65, 90.0 |
| No. of unique reflections | 32243 | 12599 | 39961 |
| Resolution (Å) | 40-2.55 (2.64-2.55) | 50-3.0 (3.11-3.0) | 40-2.9 (3.0-2.9) |
| Rsyma (%) | 10.5 (48.7) | 9.8 (52.4) | 6.7 (21.4) |
| Completeness (%) | 99.4 (98.8) | 97.8 (97.3) | 92.0 (52.5) |
| Redundancy | 4.2 (3.1) | 4.8 (4.3) | 3.4 (1.8) |
| I/s(I) | 16.1 (2.0) | 16.1 (2.0) | 17.8 (2.7) |
|
| |||
| Refinement | |||
|
| |||
| Resolution (Å) | 40-2.55 | 46–3.0 | |
| No. of unique reflections | 32190 | 12547 | |
| Rwork b/Rfree c (%) | 21.9/24.8 | 22.7/28.8 | |
|
| |||
| No. atoms | |||
| Protein | 3353 | 3249 | |
| Water | 131 | 34 | |
|
| |||
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.007 | 0.012 | |
| Bond angles (deg) | 1.0 | 1.3 | |
|
| |||
| B-factors (Å2) | |||
| Protein | |||
| Nup107 | 54.1 | 64.3 | |
| Nup133D1/Nup133D2d | 70.5/144.7 | 77.0/114.4 | |
| Water | 59.3 | 63.6 | |
|
| |||
| Ramachandran | |||
| Most favored regions (%) | 95.4 | 91.6 | |
| Add. allowed regions (%) | 4.6 | 8.4 | |
| Outliers (%) | 0.0 | 0.0 | |
a
Rsym = Σ|Ii − <Ii>|/ΣIi, where Ii is the intensity of the ith observation and <Ii> is the mean intensity of the reflection.
b
Rwork = Σ(||Fobs| − |Fcalc||/Σ|Fobs|)
c
Rfree = R value for a randomly selected subset (10%) of the data that were not used for minimization of the crystallographic residual.
Highest resolution shell is shown in parenthesis.
d
Average B-factors are reported separately for the two domains of Nup133. D1 denotes the Nup107 interaction domain (residues 934–1008), D2 the C-terminal domain (residues 1028–1156)