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2VOV

An oxidized tryptophan facilitates copper-binding in Methylococcus capsulatus secreted protein MopE. The structure of wild-type MopE to 1.35AA

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM1A
Synchrotron siteESRF
BeamlineBM1A
Temperature [K]100
Detector technologyCCD
DetectorMARRESEARCH
Spacegroup nameI 2 2 2
Unit cell lengths72.990, 88.570, 101.430
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution28.300 - 1.350
R-factor0.194
Rwork0.193
R-free0.21100
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2vox
RMSD bond length0.007
RMSD bond angle1.141
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareMOLREP
Refinement softwareREFMAC (5.3.0021)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]28.3001.420
High resolution limit [Å]1.3501.350
Rmerge0.0400.050
Number of reflections71009
<I/σ(I)>8.61.6
Completeness [%]98.597.3
Redundancy5.25.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
17.536-45% AMMONIUM SULFATE, 0.1 M HEPES PH 7.25-7.75

223790

PDB entries from 2024-08-14

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