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4Q6N

Structural analysis of the tripeptide-bound form of Helicobacter pylori Csd4, a D,L-carboxypeptidase

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsPHOTON FACTORY BEAMLINE BL-17A
Synchrotron sitePhoton Factory
BeamlineBL-17A
Temperature [K]100
Detector technologyCCD
Collection date2013-01-28
DetectorADSC QUANTUM 270
Wavelength(s)0.9800
Spacegroup nameP 21 21 21
Unit cell lengths53.127, 66.383, 143.785
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000 - 1.550
R-factor0.20149
Rwork0.200
R-free0.22673
Structure solution methodSAD
RMSD bond length0.008
RMSD bond angle1.318
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareAutoSol
Refinement softwareREFMAC (5.6.0117)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.580
High resolution limit [Å]1.5501.550
Number of reflections71540
Completeness [%]95.796.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP7.52960.2M calcium chloride, 0.1M HEPES-NaOH, 25%(w/v) polyethylene glycol 3350, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 296K

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