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1Q34

Crystal structures of two UBC (E2) enzymes of the ubiquitin-conjugating system in Caenorhabditis elegans

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 22-ID
Synchrotron siteAPS
Beamline22-ID
Temperature [K]100
Detector technologyCCD
Collection date2002-11-10
DetectorMARRESEARCH
Wavelength(s)1.072
Spacegroup nameP 1 21 1
Unit cell lengths100.922, 37.584, 103.881
Unit cell angles90.00, 117.58, 90.00
Refinement procedure
Resolution19.740 - 2.900
R-factor0.233
Rwork0.233
R-free0.26600
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2aak
RMSD bond length0.009
RMSD bond angle1.500
Data reduction softwareHKL-2000
Data scaling softwareSCALEPACK
Phasing softwareMOLREP
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0002.870
High resolution limit [Å]2.7702.770
Rmerge0.039
Number of reflections17357
<I/σ(I)>16.2
Completeness [%]95.883.1
Redundancy2.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP9.6295PEG 8000, Calcium Acetate, Glycerol, Glycine, pH 9.6, VAPOR DIFFUSION, HANGING DROP, temperature 295K

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