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2PRJ

Binding of N-acetyl-beta-D-glucopyranosylamine to Glycogen Phosphorylase B

Replaces:  1PRJ
Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsSIEMENS
Temperature [K]298
Collection date1994-08-09
DetectorSIEMENS
Spacegroup nameP 43 21 2
Unit cell lengths128.500, 128.500, 116.300
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution18.170 - 2.300
R-factor0.181
Rwork0.181
R-free0.23700
RMSD bond length0.018

*

RMSD bond angle3.600

*

Data reduction softwareXDS
Data scaling softwareXDS
Refinement softwareX-PLOR (3.851)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]28.1702.400
High resolution limit [Å]2.3002.300
Rmerge0.055
Total number of observations62732

*

Number of reflections35730
<I/σ(I)>11.5
Completeness [%]84.0

*

46.5
Redundancy4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1unknown

*

6.716

*

GLYCOGEN PHOSPHORYLASE WAS CO-CRYSTALLISED WITH 20 MM N-ACETYL-BETA-D-GLUCOPYRANOSYLAMINE IN A MEDIUM CONSISTING OF 20-30 MG/ML ENZYME, 1 MM IMP, 1 MM SPERMINE, 10 MM BES, 3 MM DITHIOTHREITOL, 0.1 MM EDTA, 0.02% (W/V) SODIUM AZIDE, PH 6.7 AT 16 C, VAPOR DIFFUSION, HANGING DROP, temperature 289K
Crystallization Reagents
IDcrystal IDsolution IDreagent nameconcentrationdetails
111SPERMINE
211BES
311DITHIOTHREITOL
411NAN3
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
111-GlcNAc20 (mM)in a medium consisting
21enzyme20-30 (mg/ml)
31IMP1 (mM)
41spermine1 (mM)
511BES10 (mM)
611dithiothreitol3 (mM)
711EDTA0.1 (mM)
811sodium azide0.02 (%(w/v))

223166

PDB entries from 2024-07-31

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