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1HQG

CRYSTAL STRUCTURE OF THE H141C ARGINASE VARIANT COMPLEXED WITH PRODUCTS ORNITHINE AND UREA

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSSRL BEAMLINE BL7-1
Synchrotron siteSSRL
BeamlineBL7-1
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2000-06-19
DetectorMAR scanner 345 mm plate
Wavelength(s)1.08
Spacegroup nameP 32
Unit cell lengths88.200, 88.200, 106.500
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution30.000 - 2.000
R-factor0.243
Rwork0.243
R-free0.23200
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.005
RMSD bond angle22.600

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.070
High resolution limit [Å]2.0002.000
Rmerge0.0610.350
Total number of observations111757

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Number of reflections59154
<I/σ(I)>12.2
Completeness [%]94.396.9
Redundancy1.91.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP8.54

*

Kanyo, Z.F., (1992) J.Mol.Biol., 224, 1175.

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Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein16 (mg/ml)
21dropBicine50 (mM)
31drop1 (mM)
41reservoirPEG800014 (%(w/v))
51reservoirBicine50 (mM)
61reservoir1 (mM)
71reservoirsodium azide0.05 (%(w/v))

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