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5ZZV

Crystal structure of PEG-1500 crystallized Peptidyl-tRNA Hydrolase from Acinetobacter baumannii at 1.5 A resolution

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID29
Synchrotron siteESRF
BeamlineID29
Temperature [K]100
Detector technologyPIXEL
Collection date2018-05-13
DetectorDECTRIS PILATUS3 S 6M
Wavelength(s)0.9095
Spacegroup nameP 21 21 2
Unit cell lengths109.025, 34.383, 58.659
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution39.930 - 1.570
R-factor0.17177
Rwork0.170
R-free0.20544
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)4fop
RMSD bond length0.019
RMSD bond angle1.888
Data reduction softwareXDS
Data scaling softwareSCALEPACK
Phasing softwareMOLREP
Refinement softwareREFMAC (5.8.0158)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]39.9301.630
High resolution limit [Å]1.5701.570
Rmeas0.1450.145
Number of reflections2483624836
<I/σ(I)>8.78.7
Completeness [%]99.599.5
Redundancy1212
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.5298100mM HEPES, 15% PEG 1500

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