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1P29

Crystal Structure of glycogen phosphorylase b in complex with maltopentaose

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU
Temperature [K]293
Detector technologyIMAGE PLATE
Collection date2002-01-01
DetectorRIGAKU RAXIS IV
Wavelength(s)1.5418
Spacegroup nameP 43 21 2
Unit cell lengths128.599, 128.599, 116.348
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution30.000

*

- 2.200
R-factor0.182
Rwork0.182
R-free0.21500
Structure solution methodFOURIER SYNTHESIS
Starting model (for MR)1gfz
RMSD bond length0.006
RMSD bond angle21.600

*

Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.240
High resolution limit [Å]2.2002.200
Rmerge0.079

*

0.426

*

Total number of observations442007

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Number of reflections49992
<I/σ(I)>12.72.8
Completeness [%]95.985
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1unknown

*

6.7295Oikonomakos, N.G., (2000) J.Biol.Chem., 275, 34566.

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
111enzyme25 (mg/ml)
211flavopiridol1 (mM)
311dithiothreitol3 (mM)
411Bes10 (mM)
511EDTA0.1 (mM)
611sodium azide0.02 (%)
711spermine1 (mM)or 10 mM magnesium acetate
811glucose50 (mM)

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PDB entries from 2024-05-15

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