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1E24

LYSYL-TRNA SYNTHETASE (LYSU) HEXAGONAL FORM complexed with lysine and ATP and MN2+

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSRS BEAMLINE PX9.6
Synchrotron siteSRS
BeamlinePX9.6
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1998-09-15
DetectorMARRESEARCH
Spacegroup nameP 61 2 2
Unit cell lengths143.600, 143.600, 177.230
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution25.000 - 2.350
R-factor0.182
Rwork0.182
R-free0.24900
Structure solution methodOTHER
RMSD bond length0.006
RMSD bond angle22.900

*

Data reduction softwareMOSFLM
Data scaling softwareCCP4
Phasing softwareX-PLOR (3.1)
Refinement softwareX-PLOR (3.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]65.0002.480
High resolution limit [Å]2.3502.350
Rmerge0.0720.182
Total number of observations217414

*

Number of reflections45104
<I/σ(I)>15.57.3
Completeness [%]99.499
Redundancy4.94.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

7.5

*

THE PROTEIN WAS CONCENTRATED TO 12 MG/ML IN THE PRESENCE OF 5MM LYSINE AND WAS CRYSTALLISED FROM 0.1 M PIPES PH 6.8, 0.5 M LICL, 20% PEG 4K, 17% GLYCEROL; THEN, A SMALL AMOUNT OF A SOLUTION CONTAINING ATP AND MNCL2 WAS ADDED TO THE DROP TO GET A FINAL CONCENTRATION OF ABOUT 5 MM.
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein12 (mg/ml)
21dropHEPES20 (mM)
31droplysine5 (mM)
41dropbeta-mercaptoethanol2 (mM)
51reservoirPEG200020 (%)
61reservoir0.5 (M)
71reservoirPIPES0.1 (M)

219140

PDB entries from 2024-05-01

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