Table 3. Statistics of electron crystallographic structures for aquaporin-0 (AQP0) in sphingomyelin/cholesterol membranes.
| 2SM:1Chol | 1SM:2Chol | |
|---|---|---|
| Crystal parameters | ||
| Space group | p422 | |
| Unit cell constants | a=b=65.5 Å, γ=90° | |
| Assumed thickness | 200 Å | |
| Electron diffraction | ||
| Diffraction patterns | 214 | 241 |
| (0°:16; 20°:19; 45°:77; 60°:84; 65°:17; 70°:1) | (0°:15; 20°:18; 45°:51; 60°:86; 65°:30; 70°:41) | |
| Maximum tilt angle | 71.72° | 72.35° |
| Upper resolution limit for merging | 2.3 Å | 2.3 Å |
| R Friedel | 0.149 | 0.138 |
| R merge | 0.216 | 0.199 |
| Observed amplitudes | 122,501 | 127,703 |
| Unique reflections | 16,437 | 17031 |
| Minimum of Fobs/Sigmaobs | 1.33 | 1.33 |
| Fourier space sampled | 87.0% | 90.7% |
| Multiplicity | 6.2 | 6.3 |
| (2.3 Å: 4.9) | (2.3 Å: 4.6) | |
| Crystallographic refinement | ||
| Resolution range | 13.8–2.35 Å | 11.8–2.35 Å |
| R work /R free * | 0.260/0.286 | 0.262/0.287 |
| Atoms | ||
| Protein | 1663 | 1663 |
| Lipids | 336 | 341 |
| Water | 11 | 11 |
| RMS deviation | ||
| Bond length (Å) | 0.008 | 0.005 |
| Bond angle (degrees) | 1.096 | 0.842 |
| Model validation | ||
| Clashscore | 8.86 | 6.98 |
| MolProbity | 1.79 | 1.79 |
| Rotamer outliers (%) | 0.00 | 0.60 |
| C-beta deviation | 0 | 0 |
| Ramachandran plot (%) | ||
| Disallowed | 0.00 | 0.00 |
| Allowed | 4.59 | 5.96 |
| Favored | 95.41 | 94.04 |
*
Rfree was calculated from randomly selected 10% of total reflections, and Rwork was calculated from the remaining 90% of reflections.