4FEF
The crystal structures of several mutants of pleurotus eryngii versatile peroxidase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-04-21 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.8726 |
Spacegroup name | I 41 |
Unit cell lengths | 96.584, 96.584, 98.065 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 68.810 - 2.000 |
R-factor | 0.1391 |
Rwork | 0.138 |
R-free | 0.17632 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2vka |
RMSD bond length | 0.034 |
RMSD bond angle | 2.100 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 68.810 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.110 | 0.411 |
Number of reflections | 30379 | |
<I/σ(I)> | 11.5 | 3.7 |
Completeness [%] | 100.0 | 100 |
Redundancy | 4.3 | 4.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5 | 295 | 1.4 M ammonium sulfate, 0.1 M sodium cacodilate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K |