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5GK3

Native structure of fructose 1,6-bisphosphate aldolase from Escherichia coli at 1.8 Angstrom resolution

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsPAL/PLS BEAMLINE 5C (4A)
Synchrotron sitePAL/PLS
Beamline5C (4A)
Temperature [K]100
Detector technologyCCD
Collection date2015-11-28
DetectorADSC QUANTUM 315r
Wavelength(s)0.979
Spacegroup nameP 1 21 1
Unit cell lengths72.251, 72.837, 73.361
Unit cell angles90.00, 103.09, 90.00
Refinement procedure
Resolution50.000 - 1.800
R-factor0.15625
Rwork0.155
R-free0.18865
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1dos
RMSD bond length0.022
RMSD bond angle1.811
Data reduction softwareHKL-2000
Data scaling softwareHKL-3000
Phasing softwarePHASER
Refinement softwareREFMAC (5.8.0135)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.850
High resolution limit [Å]1.8001.800
Rmerge0.0540.424
Number of reflections68416
<I/σ(I)>36.75.2
Completeness [%]99.9100
Redundancy5.25.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP72870.2M ammonium acetate, 5% fructose 1,6-bisphosphatase, 0.1M Tris pH 7.0, and 15% PEG 4000

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