1OO5
Studies on the Nitroreductase Prodrug-Activating System. Crystal Structures of the Enzyme Active Form and Complexes with the Inhibitor Dicoumarol and Dinitrobenzamide Prodrugs
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 97 |
| Detector technology | CCD |
| Collection date | 2001-07-01 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.93 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 56.970, 56.970, 265.650 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.920 - 2.500 |
| R-factor | 0.204 |
| Rwork | 0.204 |
| R-free | 0.28900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ds7 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.200 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.085 | 0.369 |
| Number of reflections | 15515 | |
| <I/σ(I)> | 10 | 1 |
| Completeness [%] | 96.2 | 89 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 277 | PEG 4000 (25%-29%), 0.1 mM sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
