2PRH
The structures of apo- and inhibitor bound human dihydroorotate dehydrogenase reveal conformational flexibility within the inhibitor binding site
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I711 |
| Synchrotron site | MAX II |
| Beamline | I711 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2004-04-27 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 1.092 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 90.550, 90.550, 122.700 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.360 - 2.400 |
| R-factor | 0.174 |
| Rwork | 0.172 |
| R-free | 0.21700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1d3g |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.263 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | CNS |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.340 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.118 | 0.417 |
| Number of reflections | 29077 | |
| <I/σ(I)> | 12 | 4.61 |
| Completeness [%] | 75.0 | 94 |
| Redundancy | 5.2 | 5.18 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.8 | 298 | 0.1M acetate, 1.6-2.4M ammonium sulphate, 30% glycerol, pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
