1JRP
Crystal Structure of Xanthine Dehydrogenase inhibited by alloxanthine from Rhodobacter capsulatus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X4A |
| Synchrotron site | NSLS |
| Beamline | X4A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-04-25 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.900 |
| Spacegroup name | P 1 |
| Unit cell lengths | 92.617, 140.728, 157.665 |
| Unit cell angles | 109.59, 105.84, 101.25 |
Refinement procedure
| Resolution | 30.000 - 3.000 |
| R-factor | 0.195 * |
| Rwork | 0.193 |
| R-free | 0.24400 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1jro |
| RMSD bond length | 0.030 |
| RMSD bond angle | 2.751 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 3.100 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.159 * | 0.741 * |
| Total number of observations | 551313 * | |
| Number of reflections | 135608 | |
| <I/σ(I)> | 10.1 | 2.1 |
| Completeness [%] | 99.1 | |
| Redundancy | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 8 | 295 | PEG, Tris, DTT, isopropanol at pH 8.0, VAPOR DIFFUSION, HANGING DROP at 295K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | PEG8000 | 8 (%) | |
| 3 | 1 | reservoir | 7.5 (mM) | ||
| 4 | 1 | reservoir | dithiothreitol | 25 (mM) | |
| 5 | 1 | reservoir | isopropanol | 3 (%) | |
| 6 | 1 | reservoir | Tris | 0.1 (M) | pH8.0 |
