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1DTO

CRYSTAL STRUCTURE OF THE COMPLETE TRANSACTIVATION DOMAIN OF E2 PROTEIN FROM THE HUMAN PAPILLOMAVIRUS TYPE 16

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineX11
Temperature [K]120
Detector technologyIMAGE PLATE
Collection date1998-05-15
DetectorMARRESEARCH
Spacegroup nameP 31 2 1
Unit cell lengths54.680, 54.680, 155.730
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution30.000 - 1.900
R-factor0.236
Rwork0.232
R-free0.30500
Structure solution methodMIR
Starting model (for MR)NONE
RMSD bond length0.013
RMSD bond angle0.026
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareMLPHARE
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0001.930
High resolution limit [Å]1.9001.900
Rmerge0.0580.339
Number of reflections21751
<I/σ(I)>25.7
Completeness [%]98.889.3
Redundancy3.72.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP8

*

291monomethylether PEG 5000, NaCl, isopropanol, triethanolamine,Tris-HCl, DTT, EDTA, pH 8.3, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein4.0-5.0 (mg/ml)
21dropTris-HCl10 (mM)
31dropdithiothreitol0.5 (mM)
41dropEDTA0.2 (mM)
51drop300 (mM)
61reservoirmPEG500011 (%)
71reservoirisopropanol5-9 (%)
81reservoirtriethanolamine0.1 (M)
91reservoir300 (mM)

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