2VKA
Site-Directed Mutagenesis of the Catalytic Tryptophan Environment in Pleurotus eryngii Versatile Peroxidase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC CCD |
Spacegroup name | I 41 |
Unit cell lengths | 96.290, 96.290, 98.530 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 26.120 - 2.000 |
R-factor | 0.146 |
Rwork | 0.144 |
R-free | 0.18500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2boq |
RMSD bond length | 0.017 |
RMSD bond angle | 1.515 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.3.0036) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.010 | 2.020 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.130 | 0.410 |
Number of reflections | 30110 | |
<I/σ(I)> | 10.72 | 2.89 |
Completeness [%] | 99.3 | 98.8 |
Redundancy | 4.15 | 4.18 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 1.4 M AMMONIUM SULFATE AND 100 MM SODIUM CACODILATE |