1EB4
Histidine Ammonia-Lyase (HAL) Mutant F329A 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 | 78.970, 116.900, 129.310 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 - 2.000 |
R-factor | 0.171 |
R-free | 0.23200 |
Structure solution method | OTHER |
RMSD bond length | 0.005 |
RMSD bond angle | 0.017 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Refinement software | SHELX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | |
High resolution limit [Å] | 2.000 | |
Rmerge | 0.134 * | 0.310 * |
Number of reflections | 39112 | |
<I/σ(I)> | 5.4 | |
Completeness [%] | 96.0 | 99 * |
Redundancy | 3.8 | 3.6 * |
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 |