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1QL6

THE CATALYTIC MECHANISM OF PHOSPHORYLASE KINASE PROBED BY MUTATIONAL STUDIES

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF
Synchrotron siteESRF
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1995-11-07
DetectorMARRESEARCH
Spacegroup nameP 21 21 21
Unit cell lengths47.560, 68.171, 112.475
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000 - 2.400
Rwork0.240
R-free0.33000
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2phk
RMSD bond length0.013
RMSD bond angle0.042
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareAMoRE
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.000
High resolution limit [Å]2.400
Rmerge0.048

*

0.221

*

Total number of observations40795

*

Number of reflections12745
<I/σ(I)>10.1
Completeness [%]86.678.5

*

Redundancy3.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

8.2

*

14

*

pH 6.90
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropPhk gamma trnc10-12 (mg/ml)
101reservoirHEPES/NaOH50 (mM)
111reservoir10 (mM)
121reservoirglycerol10 (%(v/v))
131reservoirdithiothreitol10 (mM)
141reservoir 0.02 (%(w/v))
21dropAMPPNP3 (mM)
31dropHEPES/NaOH10 (mM)
41dropglycerol2 (%(v/v))
51dropdithiothreitol10 (mM)
61drop0.02 (%(w/v))
71dropEDTA0.1 (mM)
81drop10 (mM)
91reservoirPEG80005 (%(w/v))

237992

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