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5AE4

Structures of inactive and activated DntR provide conclusive evidence for the mechanism of action of LysR transcription factors

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID23-1
Synchrotron siteESRF
BeamlineID23-1
Temperature [K]100
Detector technologyPIXEL
DetectorDECTRIS PILATUS 6M
Spacegroup nameP 65 2 2
Unit cell lengths107.472, 107.472, 297.771
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution43.570 - 3.300
R-factor0.1908
Rwork0.188
R-free0.24030
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1utb
RMSD bond length0.004
RMSD bond angle0.863
Data reduction softwareXDS
Data scaling softwareSCALA
Phasing softwarePHASER
Refinement softwarePHENIX ((PHENIX.REFINE))
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]43.5703.480
High resolution limit [Å]3.3003.300
Rmerge0.2000.950
Number of reflections16127
<I/σ(I)>10.92.6
Completeness [%]99.7100
Redundancy5.55.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
18.50.2 M SODIUM TARTRATE, 0.2 M POTASSIUM THIOCYANATE 0.1 M TRIS-HCL PH 8.5, 20 % (W/V) PEG 8000

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PDB entries from 2024-10-30

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