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2HL0

Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with seryl-3'-aminoadenosine

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU300
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2005-11-02
DetectorMAR scanner 345 mm plate
Wavelength(s)1.5418
Spacegroup nameI 2 2 2
Unit cell lengths53.022, 77.223, 90.952
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution24.770 - 1.860
R-factor0.193
Rwork0.193
R-free0.22000
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1y2q
RMSD bond length0.006
RMSD bond angle1.400
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareCCP4 ((MOLREP))
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]25.0001.930
High resolution limit [Å]1.8601.860
Rmerge0.0630.236
Number of reflections15968
<I/σ(I)>19.653.85
Completeness [%]99.191.4
Redundancy4.63.8
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6.527730% PEG 8000, 0.2M ammonium sulphate, 0.1M sodium cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K

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