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1PYG

STRUCTURAL BASIS FOR THE ACTIVATION OF GLYCOGEN PHOSPHORYLASE B BY ADENOSINE MONOPHOSPHATE

Experimental procedure
Spacegroup nameP 21 21 2
Unit cell lengths169.900, 209.900, 123.400
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution8.000 - 3.000

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R-factor0.185

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Rwork0.185
RMSD bond length0.014
RMSD bond angle3.200
Phasing softwareX-PLOR
Refinement softwareX-PLOR
Data quality characteristics
 Overall
High resolution limit [Å]3.000

*

Rmerge0.053

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Total number of observations522198

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Number of reflections77728

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Completeness [%]99.2

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Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion

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6.8

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Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein5-7 (mg/ml)
101reservoirPEG80008 (%)
21droptriethanolamine50 (mM)
31drop100 (mM)
41dropethylenediaminetetraacetic acid1 (mM)
51dropdithiothreitol1 (mM)
61dropmagnesium acetate2.5 (mM)
71dropAMP0.5 (mM)
81dropmaltoheptaose12.5 (mM)
91dropPEG80003-4 (%)

220113

PDB entries from 2024-05-22

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