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3FM1

Crystal Structure Analysis of Fungal Versatile Peroxidase from Pleurotus eryngii

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM1A
Synchrotron siteESRF
BeamlineBM1A
Temperature [K]120
Detector technologyIMAGE PLATE
Collection date2002-01-23
DetectorMAR scanner 345 mm plate
Wavelength(s)0.800
Spacegroup nameP 43
Unit cell lengths63.645, 63.645, 99.598
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution24.710 - 1.780
R-factor0.12675
Rwork0.124
R-free0.17241
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)3fkg
RMSD bond length0.019
RMSD bond angle1.622
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]25.0001.780
High resolution limit [Å]1.7401.740
Number of reflections40092
<I/σ(I)>13.22.8
Completeness [%]98.699.4
Redundancy2.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6.52989.0mg/ml protein in 10mM Na-tartrate pH 5.5, 17% PEG 10000, 200mM Zn-acetate, 100mM Na-cacodylate pH 6.5; Crystals were soaked with Mn2+; VAPOR DIFFUSION, HANGING DROP, temperature 298K

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