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4HE0

Crystal structure of human muscle fructose-1,6-bisphosphatase

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU200
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2004-12-15
DetectorRIGAKU RAXIS
Wavelength(s)1.5418
Spacegroup nameP 42 21 2
Unit cell lengths73.853, 73.853, 146.749
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution50.000 - 2.690
R-factor0.202
Rwork0.200
R-free0.25280
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1eyi
RMSD bond length0.012
RMSD bond angle1.393
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareMOLREP
Refinement softwareREFMAC
Data quality characteristics
 OverallInner shellOuter shell
Low resolution limit [Å]50.00050.0002.790
High resolution limit [Å]2.6905.7902.690
Rmerge0.1840.0830.509
Number of reflections11946
<I/σ(I)>6.6
Completeness [%]99.998.9100
Redundancy8.88.57.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.52950.1M MgCl2, 15% PEG 4000, 0.1M Hepes pH 7.5, vapor diffusion, hanging drop, temperature 295K

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