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3SVI

Structure of the Pto-binding domain of HopPmaL generated by limited thermolysin 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 lengths57.277, 57.277, 55.658
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution25.615 - 1.800
R-factor0.1874
Rwork0.186
R-free0.21780
Structure solution methodSAD
RMSD bond length0.007
RMSD bond angle1.009
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareSHELXCD
Refinement softwarePHENIX ((phenix.refine: 1.7.1_743))
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]25.6151.780
High resolution limit [Å]1.7501.750
Rmerge0.0710.428
Number of reflections9824
<I/σ(I)>43.4293.9
Completeness [%]99.9100
Redundancy9.29.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.52940.1M Hepes ph7.5, 0.1M NaCl, 1.6M Ammonium Sulphate, 0.2 mg/ml thermolysin was added to the protein mixture. Paratone-N oil was used for cryoprotection, VAPOR DIFFUSION, HANGING DROP, temperature 294K

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