5LBT
Structure of the human quinone reductase 2 (NQO2) in complex with imiquimod
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-04-08 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.976 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 57.689, 80.925, 106.198 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.400 - 1.750 |
| R-factor | 0.19909 |
| Rwork | 0.198 |
| R-free | 0.22652 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 2bzs |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.716 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.400 | 1.810 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.124 | 1.600 |
| Number of reflections | 49249 | |
| <I/σ(I)> | 6.01 | 0.05 |
| Completeness [%] | 93.0 | 75 |
| Redundancy | 4.6 | 4.7 |
| CC(1/2) | 0.995 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 293 | 0.1 M Tris HCl pH 8.5 2 M ammonium sulphate |
