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1XBR

T DOMAIN FROM XENOPUS LAEVIS BOUND TO DNA

Experimental procedure
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM14
Synchrotron siteESRF
BeamlineBM14
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1996-06
DetectorMARRESEARCH
Spacegroup nameP 21 21 21
Unit cell lengths37.900, 113.900, 149.000
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000 - 2.500
R-factor0.215
Rwork0.215
R-free0.28300
Structure solution methodMIR
RMSD bond length0.009
RMSD bond angle24.400

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareCCP4
Refinement softwareX-PLOR
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.590
High resolution limit [Å]2.5002.500
Rmerge0.136

*

Total number of observations101653

*

Number of reflections22983
<I/σ(I)>33.513.7
Completeness [%]98.998.9
Redundancy4.44.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP4.2PROTEIN WAS CRYSTALLIZED FROM 2-8% PEG 8K, 20 MM MGCL2 50 MM NA-ACETATE, PH 4.2 1MM DTT, 5 MM SPERMINE, VAPOR DIFFUSION, HANGING DROP
Crystallization Reagents
IDcrystal IDsolution IDreagent nameconcentrationdetails
111WATER
1012SPERMINE
211NACL
311HEPES
411DTT
512WATER
612PEG 8000
712MGCL2
812NA ACETATE
912DTT

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