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 |
