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3Q7H

Structure of the ClpP subunit of the ATP-dependent Clp Protease from Coxiella burnetii

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 21-ID-D
Synchrotron siteAPS
Beamline21-ID-D
Temperature [K]110
Detector technologyCCD
Collection date2009-12-10
DetectorMARMOSAIC 300 mm CCD
Wavelength(s)0.97920
Spacegroup nameP 1 21 1
Unit cell lengths101.912, 137.469, 127.784
Unit cell angles90.00, 109.03, 90.00
Refinement procedure
Resolution37.490 - 2.500
R-factor0.172
Rwork0.170
R-free0.20770
Structure solution methodSAD
RMSD bond length0.009
RMSD bond angle1.119
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareSHELXS
Refinement softwarePHENIX (1.6.4_486)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]37.5002.590
High resolution limit [Å]2.5002.500
Rmerge0.1030.563
Number of reflections115464
<I/σ(I)>17.33.4
Completeness [%]99.999.9
Redundancy6.86.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP729810% PEG400, 10mM calcium chloride, 100mM potassium chloride, 50mM HEPES, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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