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2E0T

Crystal structure of catalytic domain of dual specificity phosphatase 26, MS0830 from Homo sapiens

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsSPRING-8 BEAMLINE BL12B2
Synchrotron siteSPring-8
BeamlineBL12B2
Temperature [K]100
Detector technologyCCD
Collection date2006-07-03
DetectorRIGAKU JUPITER 210
Wavelength(s)0.976, 0.9794, 0.9642
Spacegroup nameC 1 2 1
Unit cell lengths80.721, 40.176, 49.944
Unit cell angles90.00, 110.35, 90.00
Refinement procedure
Resolution37.840 - 1.670
R-factor0.172
Rwork0.172
R-free0.21200
Structure solution methodMAD
RMSD bond length0.009
RMSD bond angle1.500
Data reduction softwareHKL-2000
Data scaling softwareSCALEPACK
Phasing softwareSOLVE
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.730
High resolution limit [Å]1.6701.670
Number of reflections17050
<I/σ(I)>22.27.45
Completeness [%]96.977.7
Redundancy3.52.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP7.62930.1M HEPES-Na (pH 7.5), 0.8M Potassium sodium tartrate tetrahydrate, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K
1VAPOR DIFFUSION, SITTING DROP7.62930.1M HEPES-Na (pH 7.5), 0.8M Potassium sodium tartrate tetrahydrate, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K
1VAPOR DIFFUSION, SITTING DROP7.62930.1M HEPES-Na (pH 7.5), 0.8M Potassium sodium tartrate tetrahydrate, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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