1OYL
Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.2 |
| Synchrotron site | ALS |
| Beamline | 5.0.2 |
| Temperature [K] | 119 |
| Detector technology | CCD |
| Collection date | 2002-10-14 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.2398 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 61.587, 54.696, 71.138 |
| Unit cell angles | 90.00, 99.57, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.590 |
| Rwork | 0.224 |
| R-free | 0.24300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1qq8 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.100 * |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.650 |
| High resolution limit [Å] | 1.590 | 1.590 |
| Rmerge | 0.038 * | 0.424 * |
| Total number of observations | 297413 * | |
| Number of reflections | 63070 * | |
| <I/σ(I)> | 17.3 | 2.51 |
| Completeness [%] | 98.4 | 93.2 |
| Redundancy | 9.5 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.4 * | 301 | ammonium sulphate, 1,6 hexanediol, HEPES, water, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 301K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | ammonium sulfate | 2.08 (M) | |
| 2 | 1 | reservoir | HEPES | 100 (mM) | pH7.5 |
| 3 | 1 | reservoir | 1,6-hexanediol | 0.9 (%(v/v)) | |
| 4 | 1 | drop | protein | 45 (mg/ml) | |
| 5 | 1 | drop | potassium phosphate | 20 (mM) | pH7.4 |
