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3MBF

Crystal structure of fructose bisphosphate aldolase from Encephalitozoon cuniculi, bound to fructose 1,6-bisphosphate

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSSRL BEAMLINE BL7-1
Synchrotron siteSSRL
BeamlineBL7-1
Temperature [K]100
Detector technologyCCD
Collection date2010-03-19
DetectorADSC QUANTUM 315
Wavelength(s)0.977400
Spacegroup nameC 2 2 21
Unit cell lengths121.460, 135.820, 61.540
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution28.030 - 2.370
R-factor0.167
Rwork0.165
R-free0.20800
Structure solution methodFOURIER SYNTHESIS
Starting model (for MR)3mdb
RMSD bond length0.016
RMSD bond angle1.499
Data reduction softwareXDS
Data scaling softwareXSCALE
Phasing softwareREFMAC
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]28.0302.430
High resolution limit [Å]2.3702.370
Rmerge0.0810.479
Number of reflections21046
<I/σ(I)>15.353.2
Completeness [%]99.799.6
Redundancy4.44.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP6.5290BASED ON PACT SCREEN CONDITION F10 WITHOUT NAKHPO4: 100MM BIS-TRIS PROPANE PH 6.5, 20% PEG 3350, 20 MM FRUCTOSE 1,6-BISPHOSPHATE, PROTEIN AT 24.7 MG/ML, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K

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