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5GK4

Native structure of fructose 1,6-bisphosphate aldolase from Escherichia coli at 2.0 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 lengths73.126, 72.893, 72.455
Unit cell angles90.00, 103.20, 90.00
Refinement procedure
Resolution50.000 - 2.000
R-factor0.15491
Rwork0.153
R-free0.20004
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1dos
RMSD bond length0.020
RMSD bond angle1.843
Data reduction softwareHKL-2000
Data scaling softwareHKL-3000
Phasing softwarePHASER
Refinement softwareREFMAC (5.8.0135)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0002.050
High resolution limit [Å]2.0002.000
Rmerge0.0470.139
Number of reflections50406
<I/σ(I)>33.812.7
Completeness [%]99.8100
Redundancy3.53.4
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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