4QGN
Human acireductone dioxygenase with iron ion and L-methionine in active center
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-06-22 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97912 |
| Spacegroup name | P 64 |
| Unit cell lengths | 105.195, 105.195, 40.822 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 37.250 - 3.050 |
| R-factor | 0.17994 |
| Rwork | 0.178 |
| R-free | 0.22790 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vr3 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.276 |
| Data reduction software | DENZO (3000: MOLREP) |
| Data scaling software | SCALEPACK (3000: MOLREP) |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.100 |
| High resolution limit [Å] | 3.050 | 3.050 |
| Rmerge | 0.182 | 0.726 |
| Number of reflections | 5073 | |
| <I/σ(I)> | 11.037 | 2.118 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 6.1 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.5 | 277 | Protein: 20 mg/ml in 50 mM Tris-HCl pH 7.8, 150mM NaCl, 2.5mM L-selenomethionine, Crystallization condition: 0.1M sodium acetate, ammonium sulfate pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
