2W23
Structure of mutant W169Y of Pleurotus eryngii versatile peroxidase (VP)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 110 |
Detector technology | CCD |
Detector | ADSC CCD |
Spacegroup name | I 41 |
Unit cell lengths | 96.740, 96.740, 98.190 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 31.010 - 1.940 |
R-factor | 0.144 |
Rwork | 0.142 |
R-free | 0.17500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2vka |
RMSD bond length | 0.013 |
RMSD bond angle | 1.322 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.4.0067) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 31.010 | 1.960 |
High resolution limit [Å] | 1.940 | 1.940 |
Rmerge | 0.080 | 0.240 |
Number of reflections | 33392 | |
<I/σ(I)> | 13.6 | 4.11 |
Completeness [%] | 99.8 | 99.4 |
Redundancy | 4.14 | 3.89 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 |