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4O0H

Crystal structure of human L-asparaginase protein with covalently linked substrate L-asparagine

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU200
Temperature [K]93
Detector technologyIMAGE PLATE
Collection date2012-05-25
DetectorRIGAKU RAXIS IV++
Wavelength(s)1.5418
Spacegroup nameP 65
Unit cell lengths59.651, 59.651, 298.517
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution29.830 - 1.970
R-factor0.16881
Rwork0.166
R-free0.23139
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)4GDV
RMSD bond length0.011
RMSD bond angle1.655
Data reduction softwareXDS
Data scaling softwareXDS
Phasing softwareMOLREP
Refinement softwareREFMAC (5.8.0049)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.090
High resolution limit [Å]1.9701.970
Number of reflections38615
<I/σ(I)>9.162.05
Completeness [%]91.980.5
Redundancy3.363.07
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP72932.2-2.5 M sodium Malonate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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