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9FHF

Crystal structure of human Glucose-6-phosphate isomerase with dihydroxyacetone phosphate ligand

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsMAX IV BEAMLINE BioMAX
Synchrotron siteMAX IV
BeamlineBioMAX
Temperature [K]100
Detector technologyPIXEL
Collection date2023-10-11
DetectorDECTRIS EIGER X 16M
Wavelength(s)0.987
Spacegroup nameP 21 21 21
Unit cell lengths80.676, 108.313, 271.497
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution45.050 - 1.800
R-factor0.1878
Rwork0.186
R-free0.22760
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.011
RMSD bond angle1.092
Data reduction softwareXDS
Data scaling softwareAimless
Phasing softwarePHASER
Refinement softwareREFMAC (1.20.1_4487)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]45.0501.864
High resolution limit [Å]1.8001.800
Rmerge0.2693.017
Rmeas0.2803.133
Rpim0.0760.836
Number of reflections22011321752
<I/σ(I)>9.741.56
Completeness [%]99.999.91
Redundancy13.513.7
CC(1/2)0.9980.695
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7295Protein buffer: 20 mM Tris pH 7.4, 30 mM NaCl, 20 dihydroxyacetone phosphate ligand. Reservoir: 21% w/v PEG3500, 0.16 M CaCl2, and 0.058 M HEPES, pH 7.0 Co-crystallization with ligand: Hanging drop: 1.5:0.5:1.5 ul - Protein (8 mg/ml):Seed stock:Reservoir. Cryoprotectant = a mixture containing the mother liquor, 24% v/v glycerol, and 15-20 mM ligand.

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