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2OEF

Open and Closed Structures of the UDP-Glucose Pyrophosphorylase from Leishmania major

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE BW7A
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineBW7A
Temperature [K]100
Detector technologyCCD
Collection date2005-02-04
DetectorMARRESEARCH
Wavelength(s)1.05
Spacegroup nameC 2 2 21
Unit cell lengths72.952, 107.661, 150.131
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution19.950 - 2.400
R-factor0.214
Rwork0.214
R-free0.26100
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.006
RMSD bond angle1.300
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]19.9502.550
High resolution limit [Å]2.4002.400
Number of reflections21635
Completeness [%]92.183.8
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP729321% PEG 3350, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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