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4E0H

Crystal structure of FAD binding domain of Erv1 from Saccharomyces cerevisiae

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSSRF BEAMLINE BL17U
Synchrotron siteSSRF
BeamlineBL17U
Temperature [K]100
Detector technologyCCD
Collection date2010-01-07
Wavelength(s)0.979
Spacegroup nameP 2 21 21
Unit cell lengths38.553, 46.599, 58.880
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution50.000 - 2.000
R-factor0.19399
Rwork0.192
R-free0.22874
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1oqc
RMSD bond length0.017
RMSD bond angle1.753
Data reduction softwareHKL-2000
Data scaling softwareSCALA
Phasing softwareAMoRE
Refinement softwareREFMAC (5.5.0072)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0002.070
High resolution limit [Å]2.0002.000
Rmerge0.0640.238
Number of reflections7532
<I/σ(I)>30.910.68
Completeness [%]99.7100
Redundancy10.410.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP8.530025% polyethylene glycol 3350, 0.2M Ammonium acetate, 0.1M Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 300K

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