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1A6Q

CRYSTAL STRUCTURE OF THE PROTEIN SERINE/THREONINE PHOSPHATASE 2C AT 2 A RESOLUTION

Experimental procedure
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BL19
Synchrotron siteESRF
BeamlineBL19
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1996-02-09
DetectorMARRESEARCH
Spacegroup nameP 31 2 1
Unit cell lengths91.020, 91.020, 105.610
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution6.000 - 2.000
R-factor0.214
Rwork0.214
Structure solution methodMIR
RMSD bond length0.011
RMSD bond angle24.370

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwarePHASES
Refinement softwareX-PLOR (3.82)
Data quality characteristics
 Overall
Low resolution limit [Å]15.000
High resolution limit [Å]2.000
Rmerge0.089
Total number of observations215022

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Number of reflections33176
<I/σ(I)>12.6
Completeness [%]95.5
Redundancy6.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion

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5100

*

drop solution was mixed with an equal volume of reservoir solution

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirpotassium phosphate50 (mM)
21reservoirPEG80008-12 (%)
31reservoirglycerol15 (%(v/v))
41reservoirdithiothreitol2 (mM)
51dropTris-HCl10 (mM)
61drop50 (mM)
71drop1 (mM)
81dropdithiothreitol2 (mM)
91dropprotein15 (mg/ml)

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