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2IV0

Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSLS BEAMLINE X06SA
Synchrotron siteSLS
BeamlineX06SA
Temperature [K]100
Detector technologyCCD
Collection date2005-07-01
DetectorMARRESEARCH
Spacegroup nameP 1 21 1
Unit cell lengths81.611, 65.405, 87.181
Unit cell angles90.00, 95.28, 90.00
Refinement procedure
Resolution86.710 - 2.500
R-factor0.199
Rwork0.196
R-free0.25400
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1v94
RMSD bond length0.016
RMSD bond angle1.785
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareMOLREP
Refinement softwareREFMAC (5.2.0005)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.640
High resolution limit [Å]2.5002.500
Rmerge0.1100.480
Number of reflections31867
<I/σ(I)>11.13.5
Completeness [%]99.8100
Redundancy4.14.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
16.30.6M ZNSO4, 0.1M NACACODYLATE, PH6.3, pH 6.30

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