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5GK7

Structure of E.Coli fructose 1,6-bisphosphate aldolase bound to Tris

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 lengths72.422, 72.671, 73.052
Unit cell angles90.00, 103.16, 90.00
Refinement procedure
Resolution50.000 - 1.800
R-factor0.16435
Rwork0.163
R-free0.19701
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1dos
RMSD bond length0.023
RMSD bond angle2.030
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
Rmerge0.0620.488
Number of reflections67264
<I/σ(I)>38.65
Completeness [%]97.796.3
Redundancy7.57.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP72870.2 M ammonium acetate, 5mM fructose 1,6-bisphosphatase, 0.1 M Tris/HCl pH 7.0, and 15% PEG 4000

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