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1HQF

CRYSTAL STRUCTURE OF THE BINUCLEAR MANGANESE METALLOENZYME ARGINASE COMPLEXED WITH N-HYDROXY-L-ARGININE

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSSRL BEAMLINE BL7-1
Synchrotron siteSSRL
BeamlineBL7-1
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2000-06-20
DetectorMAR scanner 345 mm plate
Wavelength(s)1.08
Spacegroup nameP 32
Unit cell lengths88.000, 88.000, 112.000
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution30.000 - 2.900
R-factor0.265
Rwork0.265
R-free0.28900
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.008
RMSD bond angle23.400

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0003.000
High resolution limit [Å]2.9002.900
Rmerge0.0640.302
Total number of observations31263

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Number of reflections17524

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781

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<I/σ(I)>11.4
Completeness [%]83.796.7

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Redundancy1.81.8
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP8.54

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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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PDB entries from 2024-05-15

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