4AUL
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 I02 |
Synchrotron site | Diamond |
Beamline | I02 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-10-06 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 200.958, 121.919, 124.919 |
Unit cell angles | 90.00, 115.28, 90.00 |
Refinement procedure
Resolution | 28.960 - 1.500 |
R-factor | 0.14547 |
Rwork | 0.143 |
R-free | 0.19334 |
Structure solution method | OTHER |
Starting model (for MR) | NONE |
RMSD bond length | 0.015 |
RMSD bond angle | 1.983 |
Data reduction software | XDS |
Data scaling software | SCALA |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.010 | 1.580 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.060 | 0.440 |
Number of reflections | 417266 | |
<I/σ(I)> | 6 | 1.8 |
Completeness [%] | 96.4 | 97.2 |
Redundancy | 1.9 | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5 | PROTEIN CRYSTAL WAS OBTAINED IN 6-16 % PEG400, 0.2 M POTASSIUM CHLORIDE, 0.01 M CALCIUM CHLORIDE DEHYDRATE AND 0.05 M SODIUM CACODYLATE TRIHYDRATE AT PH 5.0 |