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5F4X

Fructose-1,6-bisphosphate aldolase K229M mutant from rabbit muscle

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsNSLS BEAMLINE X29A
Synchrotron siteNSLS
BeamlineX29A
Temperature [K]100
Detector technologyCCD
Collection date2007-07-18
DetectorADSC QUANTUM 315
Wavelength(s)0.9795
Spacegroup nameP 1 21 1
Unit cell lengths83.477, 103.194, 84.527
Unit cell angles90.00, 98.66, 90.00
Refinement procedure
Resolution35.201 - 1.840
R-factor0.1464
Rwork0.146
R-free0.17390
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1zah
RMSD bond length0.007
RMSD bond angle1.055
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwarePHENIX
Refinement softwarePHENIX (1.9_1692)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]35.2011.910
High resolution limit [Å]1.8401.840
Number of reflections122560
<I/σ(I)>25.133.43
Completeness [%]99.799.7
Redundancy3.63.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.5296Sodium HEPES, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K

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