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1EFW

Crystal structure of aspartyl-tRNA synthetase from Thermus thermophilus complexed to tRNAasp from Escherichia coli

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsLURE BEAMLINE DW32
Synchrotron siteLURE
BeamlineDW32
Temperature [K]123
Detector technologyIMAGE PLATE
DetectorMARRESEARCH
Spacegroup nameP 63
Unit cell lengths251.450, 251.450, 88.700
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution15.000 - 3.000
R-factor0.246

*

Rwork0.248
R-free0.29100

*

RMSD bond length0.010
RMSD bond angle1.820

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]15.0003.110
High resolution limit [Å]3.0003.000
Rmerge0.0880.239
Number of reflections58634
<I/σ(I)>14.9
Completeness [%]91.998.3
Redundancy3.93.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion

*

7.517

*

sodium citrate, magnesium chloride, Na-HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 290.0K
Crystallization Reagents
IDcrystal IDsolution IDreagent nameconcentrationdetails
111sodium citrate
211MgCl2
311Na-HEPES
412sodium citrate
512MgCl2
612Na-HEPES
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein15 (mg/ml)
21droptRNA7.35 (mg/ml)
31reservoirsodium citrate0.7 (M)
41reservoir10 (mM)
51reservoirNa-HEPES50 (mM)

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PDB entries from 2024-04-17

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