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 method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL38B1 |
Synchrotron site | SPring-8 |
Beamline | BL38B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-04-20 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 54.065, 62.966, 107.728 |
Unit cell angles | 90.00, 100.78, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.700 |
R-factor | 0.16934 |
Rwork | 0.165 |
R-free | 0.20547 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.028 |
RMSD bond angle | 2.336 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.760 |
High resolution limit [Å] | 1.700 | 1.700 |
Number of reflections | 77319 | |
Completeness [%] | 98.7 | 95.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 6.1 | 303 | ammonium sulfate, MES, pH 6.1, VAPOR DIFFUSION, temperature 303K |