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3EI8

Crystal structure of K270N variant of LL-diaminopimelate aminotransferase from Arabidopsis thaliana complexed with LL-DAP: External aldimine form

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsALS BEAMLINE 8.3.1
Synchrotron siteALS
Beamline8.3.1
Temperature [K]100
Detector technologyCCD
Collection date2007-11-30
DetectorADSC QUANTUM 315
Wavelength(s)1.115872
Spacegroup nameP 32 2 1
Unit cell lengths102.476, 102.476, 171.680
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution39.410 - 1.600
R-factor0.16819
Rwork0.167
R-free0.18769
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2z20
RMSD bond length0.009
RMSD bond angle1.222
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareMOLREP
Refinement softwareREFMAC (5.5.0055)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]40.0001.660
High resolution limit [Å]1.6001.600
Number of reflections137740
Completeness [%]99.899.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.529845% (NH4)2SO4, 0.1 M HEPES pH 7.5, 3% PEG400, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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