2YG3
Structure-based redesign of cofactor binding in Putrescine Oxidase: wild type enzyme
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 |
Detector | ADSC QUANTUM 210 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 197.570, 79.770, 91.740 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 98.780 - 2.000 |
R-factor | 0.17646 |
Rwork | 0.175 |
R-free | 0.20102 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2v5z |
RMSD bond length | 0.014 |
RMSD bond angle | 1.411 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | CCP4 |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.100 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.100 | 0.310 |
Number of reflections | 96941 | |
<I/σ(I)> | 10.1 | 3.8 |
Completeness [%] | 99.8 | 96.2 |
Redundancy | 3.7 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.4 | 100MM MES PH 6.4, 2.2M AMMONIUM SULFATE, 100MM SODIUM CITRATE |