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4E0V

Structure of L-amino acid oxidase from the B. jararacussu venom

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsLNLS BEAMLINE W01B-MX2
Synchrotron siteLNLS
BeamlineW01B-MX2
Temperature [K]100
Detector technologyCCD
DetectorMARMOSAIC 225 mm CCD
Wavelength(s)1.458
Spacegroup nameP 1 21 1
Unit cell lengths66.385, 72.190, 101.527
Unit cell angles90.00, 90.90, 90.00
Refinement procedure
Resolution29.020 - 3.100
R-factor0.18541
Rwork0.181
R-free0.25931
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.013
RMSD bond angle1.667
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareMOLREP
Refinement softwareREFMAC (5.5.0066)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]29.0203.210
High resolution limit [Å]3.1003.100
Rmerge0.311
Number of reflections16155
<I/σ(I)>2.6
Completeness [%]91.379.6
Redundancy2.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP4.62910.1 M sodium acetate trihydrate pH 4.6 and 25% (w/v) polyethylene glycol 1000, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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PDB entries from 2025-12-31

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