1P3U
Crystal Structures of the NO-and CO-Bound Heme Oxygenase From Neisseria Meningitidis: Implications for Oxygen Activation
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 | 2002-07-17 |
| Detector | ADSC QUANTUM 4 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 63.033, 63.033, 101.105 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.750 |
| Rwork | 0.252 |
| R-free | 0.28700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1j77 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.323 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.810 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.035 | 0.541 |
| Total number of observations | 85041 * | |
| Number of reflections | 34991 * | |
| <I/σ(I)> | 27.3 | 4.6 |
| Completeness [%] | 86.9 * | 90.1 * |
| Redundancy | 9.6 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 298 | tris-HCl, sodium acetate, PEG 3350, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH8.5 |
| 2 | 1 | reservoir | sodium acetate | 0.2 (M) | |
| 3 | 1 | reservoir | PEG3350 | 32.5 (%) | |
| 4 | 1 | drop | protein | 23 (mg/ml) |
