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3KEA

Structure function studies of vaccinia virus host-range protein K1 reveal a novel ankyrin repeat interaction surface for K1s function

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 19-ID
Synchrotron siteAPS
Beamline19-ID
Temperature [K]77
Detector technologyCCD
Collection date2007-11-10
DetectorADSC QUANTUM 315
Wavelength(s)0.9793453, 0.9794771
Spacegroup nameP 21 21 2
Unit cell lengths95.107, 110.263, 86.259
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution39.280 - 2.300
R-factor0.212
Rwork0.210
R-free0.25400
Structure solution methodMAD
RMSD bond length0.014
RMSD bond angle1.436
Data reduction softwareHKL-3000
Data scaling softwareSCALEPACK
Phasing softwareSHELXS
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 Overall
Low resolution limit [Å]39.280
High resolution limit [Å]2.300
Number of reflections37088
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
152930.2M Natartrate, 20% PEG3350, 0.1M NaAc, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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