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1ODK

PURINE NUCLEOSIDE PHOSPHORYLASE FROM THERMUS THERMOPHILUS

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU FR-D
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2003-01-15
DetectorRIGAKU IMAGE PLATE, RAXIS-VII
Spacegroup nameP 43 21 2
Unit cell lengths131.919, 131.919, 169.906
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution19.980 - 1.900
R-factor0.18
Rwork0.180
R-free0.20800
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1je1
RMSD bond length0.005
RMSD bond angle22.800

*

Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareCNS
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0001.970
High resolution limit [Å]1.9001.900
Rmerge0.0580.267
Number of reflections116626
<I/σ(I)>264
Completeness [%]98.897.2
Redundancy7.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1microseeding

*

6.3291MICROBATCH METHOD UNDER OIL WAS USED. 15.1 MG/ML OF PROTEIN SOLUTION CONTAINING 0.02M DTT WAS MIXED WITH 1.65M SODIUM ACETATE AND 0.1M MES PH 6.3. THE CRYSTALLIZATION TEMPERATURE WAS 291 K. PARATONE-N OIL MIXED WITH 10% W/W OF GLYCEROL WAS USED FOR CRYOPROTECTION
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein15 (mg/ml)
21dropdithiothreitol0.02 (M)
31reservoirsodium acetate1.65 (M)
41reservoirMES0.1 (M)

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PDB entries from 2024-05-15

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