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3P2L

Crystal Structure of ATP-dependent Clp protease subunit P from Francisella tularensis

Experimental procedure
Experimental methodSAD
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 19-ID
Synchrotron siteAPS
Beamline19-ID
Temperature [K]100
Detector technologyCCD
Collection date2010-07-13
DetectorADSC QUANTUM 315r
Wavelength(s)0.97921
Spacegroup nameP 21 21 2
Unit cell lengths120.523, 128.823, 98.030
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution40.450 - 2.295
R-factor0.188
Rwork0.186
R-free0.22600
Structure solution methodSAD
RMSD bond length0.011
RMSD bond angle1.294
Data reduction softwareHKL-3000
Data scaling softwareHKL-3000
Phasing softwareHKL-3000
Refinement softwarePHENIX ((phenix.refine: 1.6.4_486))
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0002.340
High resolution limit [Å]2.3002.300
Number of reflections68634
<I/σ(I)>9.22.6
Completeness [%]99.999.9
Redundancy8.48.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP6.52890.2 M sodium chloride, 0.1 M sodium/potassium phosphate pH 6.5, 50 % (v/v) PEG200, VAPOR DIFFUSION, SITTING DROP, temperature 289K

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