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5GK6

Structure of E.Coli fructose 1,6-bisphosphate aldolase, Citrate bound form

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsPAL/PLS BEAMLINE 5C (4A)
Synchrotron sitePAL/PLS
Beamline5C (4A)
Temperature [K]100
Detector technologyCCD
Collection date2013-12-20
DetectorADSC QUANTUM 315r
Wavelength(s)0.979
Spacegroup nameP 1 21 1
Unit cell lengths72.033, 73.001, 73.044
Unit cell angles90.00, 104.09, 90.00
Refinement procedure
Resolution50.000 - 1.800
R-factor0.15907
Rwork0.157
R-free0.19394
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1dos
RMSD bond length0.024
RMSD bond angle1.993
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]1.7901.800
Rmerge0.1450.626
Number of reflections67229
<I/σ(I)>29.72.3
Completeness [%]98.999.7
Redundancy65.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP72870.2M ammonium acetate, 5mM aldose, 0.1M citrate buffer pH 7.0, and 15% PEG 4000

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