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3EOM

2.4 A crystal structure of native glutaryl-coa dehydrogenase from Burkholderia pseudomallei

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 21-ID-D
Synchrotron siteAPS
Beamline21-ID-D
Temperature [K]100
Detector technologyCCD
Collection date2008-01-01
DetectorMARMOSAIC 300 mm CCD
Wavelength(s)1.00
Spacegroup nameP 21 21 21
Unit cell lengths98.115, 106.768, 145.425
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution30.000 - 2.398
R-factor0.213
Rwork0.211
R-free0.26400
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.011
RMSD bond angle1.262
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwarePHASER
Refinement softwareREFMAC
Data quality characteristics
 OverallInner shellOuter shell
Low resolution limit [Å]50.00050.0002.490
High resolution limit [Å]2.3985.1702.398
Rmerge0.0840.0570.658
Number of reflections60203
<I/σ(I)>23.7
Completeness [%]99.599.198.2
Redundancy76.76.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION7.528920% PEG 3000, 0.1M HEPES pH 7.5, 0.2M NaCl, VAPOR DIFFUSION, temperature 289K

219869

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