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2VKA

Site-Directed Mutagenesis of the Catalytic Tryptophan Environment in Pleurotus eryngii Versatile Peroxidase

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-2
Synchrotron siteESRF
BeamlineID14-2
Temperature [K]100
Detector technologyCCD
DetectorADSC CCD
Spacegroup nameI 41
Unit cell lengths96.290, 96.290, 98.530
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution26.120 - 2.000
R-factor0.146
Rwork0.144
R-free0.18500
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2boq
RMSD bond length0.017
RMSD bond angle1.515
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareMOLREP
Refinement softwareREFMAC (5.3.0036)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]28.0102.020
High resolution limit [Å]2.0002.000
Rmerge0.1300.410
Number of reflections30110
<I/σ(I)>10.722.89
Completeness [%]99.398.8
Redundancy4.154.18
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
11.4 M AMMONIUM SULFATE AND 100 MM SODIUM CACODILATE

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PDB entries from 2024-10-09

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