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3VJR

Crystal structure of Peptidyl-tRNA hydrolase from Escherichia coli in complex with the CCA-acceptor-T[PSI]C domain of tRNA

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSPRING-8 BEAMLINE BL41XU
Synchrotron siteSPring-8
BeamlineBL41XU
Temperature [K]100
Detector technologyCCD
Collection date2008-07-22
DetectorMARMOSAIC 225 mm CCD
Wavelength(s)1.000
Spacegroup nameP 61
Unit cell lengths55.070, 55.070, 413.100
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution50.000 - 2.400
R-factor0.19472
Rwork0.193
R-free0.23657
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2pth
RMSD bond length0.009
RMSD bond angle1.366
Data reduction softwareXDS
Data scaling softwareXDS
Phasing softwareMOLREP
Refinement softwareREFMAC (5.5.0109)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0002.540
High resolution limit [Å]2.4002.400
Rmerge0.0560.187
Number of reflections27129
<I/σ(I)>24.948.2
Completeness [%]98.193.7
Redundancy10.98.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP5.2293100mM acetate buffer, 20% (w/v) 1,4-butanediol, 30mM glycyl-glycyl-glycine , pH 5.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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