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2AEB

Crystal structure of human arginase I at 1.29 A resolution and exploration of inhibition in immune response.

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsCHESS BEAMLINE F1
Synchrotron siteCHESS
BeamlineF1
Temperature [K]100
Detector technologyCCD
Collection date2005-04-20
DetectorADSC QUANTUM 4
Spacegroup nameP 3
Unit cell lengths91.422, 91.422, 69.637
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution? - 1.290
R-free0.15200
Structure solution methodFOURIER SYNTHESIS
Starting model (for MR)1d3v
RMSD bond length0.012
RMSD bond angle0.030
Data reduction softwareHKL-2000
Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.340
High resolution limit [Å]1.2901.290
Rmerge0.0630.560
Number of reflections150499
<I/σ(I)>9.61.85
Completeness [%]92.786
Redundancy1.41.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP7.1294PegMME 5000, Bis Tris, pH 7.1, VAPOR DIFFUSION, SITTING DROP, temperature 294.0K, pH 7.10

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