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2OO9

crystal structure of the UBA domain from human c-Cbl ubiquitin ligase

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsCHESS BEAMLINE F2
Synchrotron siteCHESS
BeamlineF2
Detector technologyCCD
Collection date2006-02-13
DetectorADSC QUANTUM 4
Spacegroup nameP 41 21 2
Unit cell lengths82.025, 82.025, 56.194
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution19.600 - 2.100
R-factor0.21838
Rwork0.216
R-free0.26009
Structure solution methodSAD
RMSD bond length0.023
RMSD bond angle1.629
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareSOLVE
Refinement softwareREFMAC (5.2.0005)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]58.0002.180
High resolution limit [Å]2.1002.100
Rmerge0.0610.313
Number of reflections11572
<I/σ(I)>18.24.9
Completeness [%]99.195.9
Redundancy7.35.7
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP8.52933.8M sodium formate, 0.1M Tris, 4% (v/v) glycerol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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