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1U9A

HUMAN UBIQUITIN-CONJUGATING ENZYME UBC9

Experimental procedure
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineBW7B
Temperature [K]281
Detector technologyIMAGE PLATE
Collection date1996-05-26
DetectorMARRESEARCH
Spacegroup nameP 1 21 1
Unit cell lengths52.040, 35.180, 58.100
Unit cell angles90.00, 111.20, 90.00
Refinement procedure
Resolution10.000 - 2.000
R-factor0.16

*

Rwork0.160
R-free0.25500

*

Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1AAK
RMSD bond length0.012
RMSD bond angle1.289
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareTNT (5E)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.030
High resolution limit [Å]2.0002.000
Rmerge0.1200.420
Number of reflections12295
<I/σ(I)>8.93.8
Completeness [%]91.094
Redundancy36.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

7.5PROTEIN WAS CRYSTALLIZED IN THE SPACE GROUP P21 FROM 9% PEG 4000, 9% ISOPROPANOL, 0.1 M HEPES, PH 7.5 SYMMETRY OPERATIONS FOR NON-STANDARD SETTING: P 21: X, Y,Z -X,Y+1/2,-Z
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein11 (mg/ml)
21drop150 (mM)
31dropDTT0.5 (mM)
41dropHEPES10 (mM)
51reservoirPEG40009 (%)
61reservoirisopropanol9 (%)
71reservoirHEPES0.1 (M)

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