5BTQ
Crystal structure of human heme oxygenase 1 H25R with biliverdin bound
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-5A |
Synchrotron site | Photon Factory |
Beamline | BL-5A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-11-04 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 61.700, 54.740, 72.510 |
Unit cell angles | 90.00, 99.37, 90.00 |
Refinement procedure
Resolution | 43.500 - 2.080 |
R-factor | 0.18503 |
Rwork | 0.183 |
R-free | 0.22818 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1n45 |
RMSD bond length | 0.012 |
RMSD bond angle | 1.906 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.500 | 2.190 |
High resolution limit [Å] | 2.080 | 2.080 |
Rmerge | 0.079 | 0.407 |
Number of reflections | 26949 | |
<I/σ(I)> | 14.4 | 3.5 |
Completeness [%] | 93.3 | 75.3 |
Redundancy | 5.1 | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 293 | 100mM HEPES 2.1M Ammonium sulfate 0.9% 1,6-hexanediol |