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 |