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3E46

Crystal structure of ubiquitin-conjugating enzyme E2-25kDa (Huntington interacting protein 2) M172A mutant

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 22-ID
Synchrotron siteAPS
Beamline22-ID
Temperature [K]100
Detector technologyCCD
Collection date2008-07-07
DetectorMARMOSAIC 300 mm CCD
Wavelength(s)0.97000
Spacegroup nameI 4
Unit cell lengths134.490, 134.490, 38.404
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution32.380 - 1.860
R-factor0.174
Rwork0.172
R-free0.21000
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2bep
RMSD bond length0.018
RMSD bond angle1.514
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareMOLREP
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.910
High resolution limit [Å]1.8601.860
Number of reflections27414
<I/σ(I)>1.98
Completeness [%]93.452.4
Redundancy41.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP6298Calcium acetate, Sodium acetate, NaCl, PEG 8000, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K

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