4AUE
Crystal structure, recombinant expression and mutagenesis studies of the bifunctional catalase-phenol oxidase from Scytalidium thermophilum
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I03 |
| Synchrotron site | Diamond |
| Beamline | I03 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-02-19 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 185.447, 216.342, 68.607 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 141.420 - 2.700 |
| R-factor | 0.19522 |
| Rwork | 0.192 |
| R-free | 0.25118 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2iuf |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.620 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.930 | 2.850 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.100 | 0.450 |
| Number of reflections | 76826 | |
| <I/σ(I)> | 13.3 | 4 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 6.5 | 6.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.8 | PROTEIN CRYSTAL WAS OBTAINED IN 22% PEG-2000 AT PH 6.8 100MM BIS-TRIS BUFFER WITH 0.1M BARIUM CHLORIDE |
