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1L6I

Crystal Structure of the Maltodextrin Phosphorylase complexed with the products of the enzymatic reaction between glucose-1-phosphate and maltopentaose

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsELETTRA BEAMLINE 5.2R
Synchrotron siteELETTRA
Beamline5.2R
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2001-02-08
DetectorMARRESEARCH
Wavelength(s)1.2
Spacegroup nameP 21 21 21
Unit cell lengths75.331, 105.937, 218.895
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000 - 2.200
R-factor0.2

*

Rwork0.197
R-free0.24300

*

Structure solution methodFOURIER SYNTHESIS
Starting model (for MR)1l5v
RMSD bond length0.021

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RMSD bond angle1.900

*

Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareDM
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]19.0002.300
High resolution limit [Å]2.2002.200
Rmerge0.1900.360
Total number of observations413101

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Number of reflections81626
<I/σ(I)>8.42.5
Completeness [%]91.487.4
Redundancy5.14.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

8.5291PEG 4000, TRIS, Lithium Chloride, Glucose-1-phosphate, pH 8.5, temperature 291K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein6.0 (mg/ml)
21dropGlc1P100 (mM)
31reservoirPEG400027 (%(w/v))
41reservoir0.1 (M)
51reservoirTris0.1 (M)pH8.5

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PDB entries from 2024-05-01

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