2AXQ
Apo histidine-tagged saccharopine dehydrogenase (L-Glu forming) from Saccharomyces cerevisiae
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH3R |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2003-08-18 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 85.279, 85.279, 141.977 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 39.850 - 1.700 |
| R-factor | 0.2 |
| Rwork | 0.198 |
| R-free | 0.24000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1e5l used monomer backbone only |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.407 |
| Data reduction software | CrystalClear (D*TREK (MSC/RIGAKU)) |
| Data scaling software | d*TREK (9.2D) |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.850 | 1.760 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.056 | 0.368 |
| Number of reflections | 64775 | |
| <I/σ(I)> | 15.8 | 4.3 |
| Completeness [%] | 97.6 | 95.9 |
| Redundancy | 7.18 | 4.98 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 298 | 1.2M Ammonium sulfate, 25mM Bis-Tris, 6.5-7mg/mL enzyme, 50mM Tris-HCl pH 8.0, 150mM KCl, 75mM imidazole, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |






