1R56
UNCOMPLEXED URATE OXIDASE FROM ASPERGILLUS FLAVUS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | LURE BEAMLINE DW32 |
| Synchrotron site | LURE |
| Beamline | DW32 |
| Temperature [K] | 283 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 82.590, 141.843, 134.959 |
| Unit cell angles | 90.00, 92.69, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.300 |
| Rwork | 0.162 |
| R-free | 0.21400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1UOX |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.275 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | EPMR |
| Refinement software | BUSTER-TNT |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 32.000 | |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.426 | |
| Number of reflections | 136450 | |
| <I/σ(I)> | 12.3 | 3.6 |
| Completeness [%] | 99.2 | 98.3 |
| Redundancy | 5.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 291 | 8.5MG/ML PROTEIN, 5-7% W/V PEG 8000, 100MM TRIS/HCL, temperature 291K, pH 8.00 |






