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THE BISPHOSPHATASE DOMAIN OF THE BIFUNCTIONAL RAT LIVER 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE

Experimental procedure
Source typeSYNCHROTRON
Source detailsNSLS BEAMLINE X4A
Synchrotron siteNSLS
BeamlineX4A
Temperature [K]95
Detector technologyIMAGE PLATE
Collection date1997-05-05
DetectorFUJI
Spacegroup nameP 1 21 1
Unit cell lengths48.230, 56.520, 90.900
Unit cell angles90.00, 94.48, 90.00
Refinement procedure
Resolution20.000 - 2.200
R-factor0.204
Rwork0.204
R-free0.28600
RMSD bond length0.012
RMSD bond angle23.466

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Data reduction softwareDENZO
Phasing softwareX-PLOR
Refinement softwareX-PLOR
Data quality characteristics
 Overall
Low resolution limit [Å]20.000

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High resolution limit [Å]2.200

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Rmerge0.033

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Number of reflections20142
Completeness [%]78.3
Redundancy8.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

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7

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Lee, Y.H., (1996) Biochemistry, 35, 6010.

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Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein7.5 (mg/ml)
101dropwater
21dropPEG400015 (%)
31dropsodium phosphate5 (mM)
41dropdithiothreitol0.5 (mM)
51dropglycerol2.5 (%)
61reservoirPEG400030 (%)
71reservoirsodium phosphate10 (mM)
81reservoirdithiothreitol1 (mM)
91reservoirglycerol5 (%)

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