1BQD
ASPARTATE AMINOTRANSFERASE P138A/P195A DOUBLE MUTANT
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | ELLIOTT |
| Temperature [K] | 290 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-07 |
| Detector | MAR scanner 300 mm plate |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 88.490, 79.880, 89.680 |
| Unit cell angles | 90.00, 119.58, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.100 |
| R-factor | 0.205 |
| Rwork | 0.204 |
| R-free | 0.24700 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bqa |
| RMSD bond length | 0.010 |
| RMSD bond angle | 24.660 * |
| Data reduction software | XDS |
| Data scaling software | Agrovata |
| Phasing software | AMoRE |
| Refinement software | TNT (5D) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.150 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.065 | 0.280 |
| Number of reflections | 58133 | |
| <I/σ(I)> | 10.1 | 3.2 |
| Completeness [%] | 91.3 | 88.3 |
| Redundancy | 2.6 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 | pH 7.5 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | drop | potassium phosphate | 10 (mM) | |
| 3 | 1 | drop | PLP | 0.010 (mM) | |
| 4 | 1 | drop | K2-EDTA | 2 (mM) | |
| 5 | 1 | drop | dithiothreitol | 0.5 (mM) | |
| 6 | 1 | reservoir | ammonium sulfate | 1.9-2.1 (M) | |
| 7 | 1 | reservoir | 2-mercaptoethanol | 0.2 (M) | |
| 8 | 1 | reservoir | PEG400 | 2 (%) |
