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2HL2

Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with an analog of seryladenylate

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU300
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2005-11-06
DetectorMAR scanner 345 mm plate
Wavelength(s)1.5418
Spacegroup nameP 21 21 21
Unit cell lengths39.652, 67.363, 98.588
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution24.840 - 2.600
R-factor0.213
Rwork0.213
R-free0.29500
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1y2q
RMSD bond length0.007
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]25.0002.690
High resolution limit [Å]2.6002.600
Rmerge0.0800.409
Number of reflections8487
<I/σ(I)>14.752.12
Completeness [%]97.886.3
Redundancy3.62.8
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6.527725% PEG 3350, 0.1M bis-tris, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K

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