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2ASV

X-Ray studies on protein complexes: Enzymatic catalysis in Crystals of E. coli Maltodextrin Phosphorylase (MalP)

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsELETTRA BEAMLINE 5.2R
Synchrotron siteELETTRA
Beamline5.2R
Temperature [K]100
Detector technologyCCD
Collection date2004-03-31
DetectorMARRESEARCH
Wavelength(s)1.2
Spacegroup nameP 21 21 21
Unit cell lengths74.327, 104.723, 214.787
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution15.000 - 1.950
R-factor0.18168
Rwork0.179
R-free0.22604
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1l5v
RMSD bond length0.019
RMSD bond angle1.633
Data scaling softwareCCP4 ((SCALA))
Refinement softwareREFMAC (5.1.24)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]15.0002.060
High resolution limit [Å]1.9501.950
Rmerge0.1190.476
Number of reflections119849
<I/σ(I)>10.11.8
Completeness [%]97.891.1
Redundancy3.92.7
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP8.5298PEG 4000, lithium chloride, (hydroxymethyl) aminomethane, maltopentaose, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

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