Table 1.
hVPS4B crystal structure statistics
| |
SeMet-hVPS4B |
|---|---|
| Data collection statistics | |
| Space group | P65 |
| Cell dimensions (Å) | a=88.1 Å |
| c=112.6 Å | |
| Resolution limit (Å)a | 30.00–2.80 (2.95–2.80) |
| No. of reflections measured | 133 252 (19 859) |
| No. of unique reflections | 12 140 |
| Completeness (%) | 99.3 (99.3) |
| I/σ(I) | 9.7 (2.6) |
| Rmergeb | 0.058 (0.285) |
| Refinement statistics | |
| Resolution (Å) | 2.8 (2.873-2.80) |
| R-valuec | 0.192 (0.303) |
| Rfreed | 0.260 (0.411) |
| R.m.s.d. bonds (Å) | 0.018 |
| R.m.s.d. angles (deg) | 1.962 |
| No. of reflections | 10 917 (822) |
| No. of reflections Free R | 1190 (95) |
| No. of waters/sulfates | 9/2 |
| B-factors (Å2) protein/water/sulfate | 52.9/33.2/45.3 |
| % Residues in most favored phi–psi regionse | 87.8 |
| % Residues in additional phi–psi regionse | 12.2 |
| aThe single molecule in the asymmetric unit lacked defined density for residues 1–122 (omitted from model) and 200–211 and 239–247 (included with zero occupancy). | |
| bRmerge=∑∣I−IAverage∣/∑I, where I is the intensity of an individual measurement and IAverage is the average intensity from multiple observations. | |
| cR-value=100∑∣∣F(obs)∣–∣F(calc)∣∣/∑∣F(obs)∣. | |
| dRfree=R-value for a randomly selected subset (10%; 1190 reflections) of the data that were not used for minimization of the crystallographic residual. | |
| eStereochemistry was assessed with PROCHECK (Laskowski et al, 1993). | |