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3RLA

ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION

Experimental procedure
Source typeROTATING ANODE
Source detailsRIGAKU RUH2R
Temperature [K]298
Detector technologyIMAGE PLATE
Collection date1995-01
DetectorRIGAKU RAXIS II
Spacegroup nameP 32
Unit cell lengths89.000, 89.000, 115.400
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution15.000 - 2.540
R-factor0.194
Rwork0.194
R-free0.28200
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)RAT LIVER ARGINASE
RMSD bond length0.013
RMSD bond angle24.300

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Data reduction softwareMOSFLM
Phasing softwareX-PLOR (3.1)
Refinement softwareX-PLOR (3.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]8.0002.600
High resolution limit [Å]2.5002.540
Rmerge0.1050.400
Total number of observations65410

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Number of reflections26381
<I/σ(I)>4.33.9
Completeness [%]74.079.5
Redundancy2.52.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, sitting drop

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8.54

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12 - 18% PEG 8000, 50 MM BICINE PH = 8.5, 0.05% AZIDE, 1 MM MNCL2
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropenzyme3-4 (mg/ml)
21dropBicine50 (mM)
31dropPEG80007-8 (%)
41dropsodium azide0.025 (%)
51drop0.5 (mM)
61reservoirBicine50 (mM)
71reservoirPEG800014-16 (%)
81reservoirsodium azide0.05 (%)
91reservoir1 (mM)

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PDB entries from 2024-05-01

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