1GKJ
Histidine Ammonia-Lyase (HAL) Mutant Y280F from Pseudomonas putida
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUB200 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 78.560, 116.672, 129.481 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.000 - 1.700 |
| R-factor | 0.198 |
| R-free | 0.23600 |
| Structure solution method | OTHER |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.025 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Refinement software | SHELX |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.000 | |
| High resolution limit [Å] | 1.700 | |
| Rmerge | 0.073 * | 0.180 * |
| Number of reflections | 64075 | |
| <I/σ(I)> | 6.6 | |
| Completeness [%] | 98.0 | 96 * |
| Redundancy | 2.9 | 2.8 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 3.85 * | Schwede, T.F., (1999) Protein Eng., 12, 151. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 12 (mg/ml) | |
| 2 | 1 | reservoir | sodium potassium phosphate | 1.6 (M) | |
| 3 | 1 | reservoir | HEPES | 0.1 (M) | |
| 4 | 1 | reservoir | EDTA | 1.5 (mM) | |
| 5 | 1 | reservoir | dioxane | 3 (%) | pH3.85 |
