1YLR
The structure of E.coli nitroreductase with bound acetate, crystal form 1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-09-19 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.934 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 57.580, 57.580, 263.180 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 56.250 - 1.700 |
R-factor | 0.17135 |
Rwork | 0.170 |
R-free | 0.19775 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1icr |
RMSD bond length | 0.010 |
RMSD bond angle | 1.185 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | CNS |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 56.250 | 1.790 |
High resolution limit [Å] | 1.700 | 1.700 |
Number of reflections | 47753 | |
<I/σ(I)> | 3.6 | 1.6 |
Completeness [%] | 99.9 | 98.8 |
Redundancy | 8 | 6.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 291 | PEG4000, ethylene glycol, nicotinic acid, sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K |