1R3R
Uroporphyrinogen Decarboxylase with mutation D86N
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2003-06-15 |
| Detector | RIGAKU RAXIS IIC |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 102.735, 102.735, 73.426 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 * - 1.850 |
| R-factor | 0.16212 |
| Rwork | 0.161 |
| R-free | 0.19200 * |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 1uro |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.690 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 * | 1.920 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.083 | 0.437 |
| Total number of observations | 175858 * | |
| Number of reflections | 36928 | |
| <I/σ(I)> | 9 | 2.8 |
| Completeness [%] | 96.0 | 79.8 * |
| Redundancy | 5 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 7.5 * | 21 * | Phillips, J.D., (1997) Protein Sci., 6, 1343. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 6 (mg/ml) | |
| 2 | 1 | drop | Tris | 50 (mM) | pH7.5 |
| 3 | 1 | drop | glycerol | 10 (%) | |
| 4 | 1 | drop | beta-mercaptoethanol | 1 (mM) | |
| 5 | 1 | reservoir | MPD | 16 (%) | |
| 6 | 1 | reservoir | MES | 0.1 | pH6.0 |
