4GF7
Crystal structure of 2-Methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO), unliganded form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44XU |
| Synchrotron site | SPring-8 |
| Beamline | BL44XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-05-25 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 0.9 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 49.363, 131.287, 132.289 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.548 - 1.581 |
| R-factor | 0.1661 |
| Rwork | 0.165 |
| R-free | 0.19200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Selenomethionine substitution of the same enzyme |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.390 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Refinement software | PHENIX ((phenix.refine: 1.7.3_928)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.610 |
| High resolution limit [Å] | 1.580 | 1.580 |
| Rmerge | 0.093 | 0.383 |
| Number of reflections | 55795 | |
| <I/σ(I)> | 12.3 | 6.1 |
| Completeness [%] | 94.6 | 95.5 |
| Redundancy | 8.5 | 8.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 8% PEG 8000, 0.1M Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
