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3TJY

Structure of the Pto-binding domain of HopPmaL generated by limited chymotrypsin digestion

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 19-ID
Synchrotron siteAPS
Beamline19-ID
Temperature [K]100
Detector technologyCCD
Collection date2009-07-10
DetectorADSC QUANTUM 315
Wavelength(s)0.97942
Spacegroup nameP 41 21 2
Unit cell lengths57.427, 57.427, 54.800
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution25.682 - 1.700
R-factor0.1894
Rwork0.188
R-free0.21740
Structure solution methodSAD
RMSD bond length0.009
RMSD bond angle1.152
Refinement softwarePHENIX ((phenix.refine: 1.7.1_743))
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]25.6821.680
High resolution limit [Å]1.6501.650
Rmerge0.0800.501
Number of reflections11555
<I/σ(I)>42.1333.7
Completeness [%]99.9100
Redundancy9.39.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6.52940.1M Bis-Tris pH 6.5 plus 1.5M Ammonium Sulphate. 0.03 mg/ml chymotrypsin was added to the protein prior to adding crystallization liquor. Crystals were cryoprotected with Paratone-N oil , VAPOR DIFFUSION, HANGING DROP, temperature 294K

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