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3P09

Crystal Structure of Beta-Lactamase from Francisella tularensis

Experimental procedure
Experimental methodSAD
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 19-ID
Synchrotron siteAPS
Beamline19-ID
Temperature [K]100
Detector technologyCCD
Collection date2010-08-11
DetectorADSC QUANTUM 315r
Wavelength(s)0.97921
Spacegroup nameP 21 21 2
Unit cell lengths77.652, 143.466, 46.890
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution40.720 - 1.898
R-factor0.164
Rwork0.162
R-free0.20700
Structure solution methodSAD
RMSD bond length0.007
RMSD bond angle1.024
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]50.0001.930
High resolution limit [Å]1.9001.900
Number of reflections41541
<I/σ(I)>8.62
Completeness [%]98.483.3
Redundancy7.95.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP6.52890.2 M Lithium sulfate monohydrate, 0.1 M BIS-TRIS pH 6.5, 25 % w/v Polyehtlyene glycol 3350, VAPOR DIFFUSION, SITTING DROP, temperature 289K

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