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4OLJ

Crystal structure of Arg119Gln mutant of Peptidyl-tRNA Hydrolase from Acinetobacter Baumannii at 1.49 A resolution

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM14
Synchrotron siteESRF
BeamlineBM14
Temperature [K]77
Detector technologyCCD
Collection date2013-11-29
DetectorMARRESEARCH
Wavelength(s)0.97
Spacegroup nameP 21 21 21
Unit cell lengths34.088, 65.834, 76.121
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution49.790 - 1.490
R-factor0.15967
Rwork0.158
R-free0.19243
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)4lwq
RMSD bond length0.029
RMSD bond angle2.429
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareAMoRE
Refinement softwareREFMAC (5.5.0109)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.520
High resolution limit [Å]1.4901.490
Number of reflections26963
<I/σ(I)>32.92.1
Completeness [%]99.194.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.529850mM HEPES, PEG 400, PEG 1500, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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