1KQB
Structure of Nitroreductase from E. cloacae complex with inhibitor benzoate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 115 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-12-15 |
| Detector | RIGAKU RAXIS IV |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 52.840, 79.310, 96.920 |
| Unit cell angles | 90.00, 93.69, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.800 |
| R-factor | 0.189 * |
| Rwork | 0.188 |
| R-free | 0.21800 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.100 |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.880 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.065 | 0.162 |
| Number of reflections | 72079 | |
| <I/σ(I)> | 20.3 | 8.3 |
| Completeness [%] | 97.5 * | 93.5 * |
| Redundancy | 3.74 | 3.51 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 * | 4 * | homopipes, benzoate, PEG 4000, pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 4.75 (mg/ml) | |
| 2 | 1 | drop | HEPES | 10 (mM) | pH7. |
| 3 | 1 | drop | 50 (mM) | ||
| 4 | 1 | reservoir | homopipes | 100 (mg/ml) | pH4.8 |
| 5 | 1 | reservoir | acetate | 25 (mM) | |
| 6 | 1 | reservoir | PEG4000 | 15 (%) |
