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5CEV

ARGINASE FROM BACILLUS CALDEVELOX, L-LYSINE 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 lengths106.400, 277.000, 138.800
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution8.000 - 2.500
R-factor0.212

*

Rwork0.212
R-free0.26100
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)REFINED MODEL FOR THE PH 8.5 NATIVE STRUCTURE: 2CEV
RMSD bond length0.011
RMSD bond angle1.470
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareX-PLOR (3.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0002.700
High resolution limit [Å]2.5002.500
Rmerge0.0670.188
Total number of observations424670

*

Number of reflections68127
<I/σ(I)>184.8
Completeness [%]94.972.7
Redundancy6.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP8.5MIXING 2 UL PROTEIN WITH 2 UL RESERVOIR SOLUTION PROTEIN SOLUTION 27 MG/ML PROTEIN, 10 MM MOPS, PH 7.5 RESERVOIR SOLUTION 28% MONOMETHYLPEG 2000, 5 MM MNCL2, 10 MM GUANIDINE HYDROCHLORIDE, 10 MM L-LYSINE, IN 0.05 M BISTRISPROPANE/HCL, PH 8.5 , VAPOR DIFFUSION, HANGING DROP
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirmmPEG200028 (%)
21reservoirguanidine hydrochloride10 (mM)
31reservoir5 (mM)
41reservoirBTP/HCl50 (mM)
51reservoirL-lysine10 (mM)

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