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 |