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2EH6

Crystal structure of acetylornithine aminotransferase from Aquifex aeolicus VF5

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSPRING-8 BEAMLINE BL26B1
Synchrotron siteSPring-8
BeamlineBL26B1
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2006-11-24
DetectorRIGAKU RAXIS V
Wavelength(s)1.0
Spacegroup nameI 2 2 2
Unit cell lengths101.094, 124.700, 131.614
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution30.000 - 1.900
R-factor0.198
Rwork0.198
R-free0.22100
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2e54
RMSD bond length0.006
RMSD bond angle1.200
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareMOLREP
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0001.970
High resolution limit [Å]1.9001.900
Rmerge0.0590.402
Number of reflections65412
<I/σ(I)>15.14.7
Completeness [%]100.0100
Redundancy7.17
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1MICROBATCH729530%(v/v) Jeffamine ED-2001, 0.1M HEPES, pH 7.0, microbatch, temperature 295K

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