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2D1G

Structure of Francisella tularensis Acid Phosphatase A (AcpA) bound to orthovanadate

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsALS BEAMLINE 8.3.1
Synchrotron siteALS
Beamline8.3.1
Temperature [K]160
Detector technologyCCD
Collection date2004-07-01
DetectorADSC QUANTUM 210
Wavelength(s)1.127129
Spacegroup nameC 2 2 21
Unit cell lengths112.081, 144.399, 123.859
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution44.280 - 1.750
Rwork0.198
R-free0.23100
Structure solution methodSAD
RMSD bond length0.012
RMSD bond angle1.683
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareSHARP
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.810
High resolution limit [Å]1.7501.750
Rmerge0.0470.357
Number of reflections98137
Completeness [%]97.2
Redundancy4.14
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP6298PEG 1500, pH 6, VAPOR DIFFUSION, SITTING DROP, temperature 298K
1VAPOR DIFFUSION, SITTING DROP6298PEG 1500, pH 6, VAPOR DIFFUSION, SITTING DROP, temperature 298K
1VAPOR DIFFUSION, SITTING DROP6298PEG 1500, pH 6, VAPOR DIFFUSION, SITTING DROP, temperature 298K

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