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4CEV

ARGINASE FROM BACILLUS CALDEVELOX, L-ORNITHINE COMPLEX

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU200
Temperature [K]113
Detector technologyIMAGE PLATE
Collection date1997-01
DetectorRIGAKU
Spacegroup nameC 2 2 21
Unit cell lengths106.600, 277.300, 139.700
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution8.000 - 2.700
R-factor0.203

*

Rwork0.203
R-free0.27400
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)REFINED MODEL FOR THE PH 8.5 NATIVE STRUCTURE: 2CEV
RMSD bond length0.010
RMSD bond angle1.420
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareX-PLOR (3.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0002.900
High resolution limit [Å]2.7002.700
Rmerge0.0970.219
Total number of observations161259

*

Number of reflections53853
<I/σ(I)>10.13
Completeness [%]93.582.4
Redundancy3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP8.5RESERVOIR SOLUTION 28% MONOMETHYLPEG 2000, 5 MM MNCL2, 10 MM GUANIDINE HYDROCHLORIDE, 10 MM D/L-ORNITHINE,IN 0.05 M BISTRISPROPANE/HCL,PH 8.5 27 MG/ML PROTEIN, 10 MM MOPSm, PH 7.5 , VAPOR DIFFUSION, HANGING DROP
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirmmPEG200028 (%)
21reservoirguanidine hydrochloride10 (mM)
31reservoir5 (mM)
41reservoirBTP/HCl50 (mM)
51reservoirD/L-ornithine10 (mM)

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PDB entries from 2024-05-15

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