2YG4
Structure-based redesign of cofactor binding in Putrescine Oxidase: wild type bound to Putrescine
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 | 198.590, 80.610, 92.120 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 34.610 - 2.300 |
| R-factor | 0.15886 |
| Rwork | 0.157 |
| R-free | 0.19742 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2yg3 |
| RMSD bond length | 0.023 |
| RMSD bond angle | 1.985 |
| 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] | 34.600 | 2.400 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.010 | 0.390 |
| Number of reflections | 66382 | |
| <I/σ(I)> | 8.7 | 3.8 |
| Completeness [%] | 99.8 | 99.4 |
| Redundancy | 3.8 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.4 | pH 6.4 |
