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4GPH

Structure of HmuO, heme oxygenase from Corynebacterium diphtheriae, in complex with the putative reaction intermediates between Fe3+-biliverdin and biliverdin (data set IV)

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSPRING-8 BEAMLINE BL38B1
Synchrotron siteSPring-8
BeamlineBL38B1
Temperature [K]100
Detector technologyCCD
Collection date2005-04-20
DetectorRIGAKU JUPITER 210
Wavelength(s)1.0
Spacegroup nameP 1 21 1
Unit cell lengths54.065, 62.966, 107.728
Unit cell angles90.00, 100.78, 90.00
Refinement procedure
Resolution30.000 - 1.700
R-factor0.16934
Rwork0.165
R-free0.20547
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.028
RMSD bond angle2.336
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Refinement softwareREFMAC (5.5.0102)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.760
High resolution limit [Å]1.7001.700
Number of reflections77319
Completeness [%]98.795.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION6.1303ammonium sulfate, MES, pH 6.1, VAPOR DIFFUSION, temperature 303K

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