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1Z2U

The 1.1A crystallographic structure of ubiquitin-conjugating enzyme (ubc-2) from Caenorhabditis elegans: functional and evolutionary significance

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 22-ID
Synchrotron siteAPS
Beamline22-ID
Temperature [K]100
Detector technologyCCD
Collection date2002-11-17
DetectorMAR CCD 165 mm
Wavelength(s)0.97
Spacegroup nameP 1 21 1
Unit cell lengths29.604, 60.457, 43.980
Unit cell angles90.00, 106.45, 90.00
Refinement procedure
Resolution30.000 - 1.100
Rwork0.131
R-free0.14930
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1qcq
RMSD bond length0.014
RMSD bond angle1.335
Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareREFMAC (refmac_5.2.0005)
Data quality characteristics
 OverallInner shellOuter shell
Low resolution limit [Å]30.00030.0001.140
High resolution limit [Å]1.1002.3701.100
Rmerge0.0550.0460.143
Number of reflections58674
Completeness [%]97.499.892.6
Redundancy5.57.43
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1capillary counter-diffusion5277.57mg/mL protein in 2mM sodium citrate, 10% (v/v) ethanol, 1.5M Sodium Chloride, pH 5.0, capillary counter-diffusion, temperature 277.5K

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