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1O5T

Crystal structure of the aminoacylation catalytic fragment of human tryptophanyl-tRNA synthetase

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsCHESS BEAMLINE F1
Synchrotron siteCHESS
BeamlineF1
Temperature [K]100
Detector technologyCCD
Collection date2003-02-10
DetectorADSC QUANTUM 4
Wavelength(s)0.916, 0.9500, 0.9790, 0.9787
Spacegroup nameP 65 2 2
Unit cell lengths82.240, 82.240, 263.560
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution29.510 - 2.500
R-factor0.245
Rwork0.245
R-free0.29600
Structure solution methodMAD
RMSD bond length0.007
RMSD bond angle1.300
Data reduction softwareHKL-2000
Data scaling softwareSCALEPACK
Phasing softwareSOLVE
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.540
High resolution limit [Å]2.5002.500
Rmerge0.0900.415
Number of reflections18911
<I/σ(I)>2
Completeness [%]98.796.3
Redundancy8.55
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP8.227716% PEG1500, 4% PEG3350, 0.2M tri-sodium citrate dihydrate, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K

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