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 |