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4FOP

Crystal Structure of Peptidyl-tRNA hydrolase from Acinetobacter baumannii at 1.86 A resolution

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM14
Synchrotron siteESRF
BeamlineBM14
Temperature [K]77
Detector technologyCCD
Collection date2012-05-18
DetectorMARRESEARCH
Wavelength(s)0.97
Spacegroup nameP 21 2 21
Unit cell lengths34.255, 57.864, 109.744
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution57.800 - 1.860
R-factor0.17785
Rwork0.175
R-free0.22795
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2pth
RMSD bond length0.021
RMSD bond angle2.036
Data reduction softwareAUTOMAR
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC (5.1.24)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]57.8001.930
High resolution limit [Å]1.8601.860
Number of reflections17986
<I/σ(I)>11.61.7
Completeness [%]99.199.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6.53100.2M HEPES Buffer, 25% PEG10000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 310K

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