1IDD
ISOCITRATE DEHYDROGENASE Y160F MUTANT APO ENZYME
Experimental procedure
| Detector technology | IMAGE PLATE |
| Collection date | 1993-07-06 |
| Detector | RIGAKU |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 105.100, 105.100, 150.300 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 * - 2.500 |
| R-factor | 0.215 |
| Rwork | 0.215 |
| R-free | 0.24600 |
| RMSD bond length | 0.021 |
| RMSD bond angle | 24.900 * |
| Data reduction software | R-AXIS |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 100.000 * |
| High resolution limit [Å] | 2.500 * |
| Rmerge | 0.090 |
| Number of reflections | 22143 |
| Completeness [%] | 87.0 |
| Redundancy | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 5.4 * | DATA WAS COLLECTED FROM TWO SEPARATE CRYSTALS AND MERGED TOGETHER WITH PROTSYS. THE MERGING R VALUE GIVEN ABOVE IS CRYSTAL TO CRYSTAL. THE MERGING R VALUE FOR INDIVIDUAL CRYSTALS IS 0.064, 0.061 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | dephosphorylated IDH | 28 (mg/ml) | |
| 2 | 1 | reservoir | ammonium sulfate | 34 (%sat) | |
| 3 | 1 | reservoir | 100 (mM) | ||
| 4 | 1 | reservoir | 35 (mM) | ||
| 5 | 1 | reservoir | citric acid | 9 (mM) | |
| 6 | 1 | reservoir | dithiothreitol | 0.2 (mM) |
