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2AW3

X-Ray studies on maltodextrin phosphorylase complexes: recognition of substrates and cathalitic mechanism of phosphorylase family

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsELETTRA BEAMLINE 5.2R
Synchrotron siteELETTRA
Beamline5.2R
Temperature [K]100
Detector technologyCCD
DetectorMARRESEARCH
Wavelength(s)1.2
Spacegroup nameP 21 21 21
Unit cell lengths75.297, 105.887, 219.520
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution15.000 - 2.200
R-factor0.17848
Rwork0.175
R-free0.23598
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1l5v
RMSD bond length0.022
RMSD bond angle1.775
Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((SCALA))
Refinement softwareREFMAC (5.1.24)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]111.8002.320
High resolution limit [Å]2.2002.200
Rmerge0.2520.852
Number of reflections88185
<I/σ(I)>7.41.9
Redundancy4.64.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP8.5298PEG4000, LITHIUM CHLORIDE, TRIS(HYDROXYMETHIL) AMINOMETHANE, MALTOPENTAOSE, LITHIUM SULPHATE, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

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