1EKV
HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL): THREE DIMENSIONAL STRUCTURE OF ENZYME INACTIVATED BY TRIS BOUND TO THE PYRIDOXAL-5'-PHOSPHATE ON ONE END AND ACTIVE SITE LYS202 NZ ON THE OTHER.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 223 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-03-17 |
| Detector | RIGAKU RAXIS IV |
| Spacegroup name | P 32 |
| Unit cell lengths | 83.740, 83.740, 104.810 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 34.270 - 2.500 * |
| R-factor | 0.195 |
| Rwork | 0.189 |
| R-free | 0.27000 * |
| Starting model (for MR) | E. COLI BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE |
| RMSD bond length | 0.012 |
| RMSD bond angle | 24.200 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (0.9) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.270 | 2.330 |
| High resolution limit [Å] | 2.300 * | 2.250 |
| Rmerge | 0.127 | 0.263 |
| Number of reflections | 37970 * | |
| <I/σ(I)> | 6.19 | |
| Completeness [%] | 82.1 * | 69.4 |
| Redundancy | 1.8 | 2.29 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 * | 298 | AMMONIUM SULPHATE, DTT, TRIS, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 2.5 (mg/ml) | |
| 2 | 1 | drop | HEPES | 50 (mM) | |
| 3 | 1 | drop | dithiothreitol | 20 (mM) | |
| 4 | 1 | drop | EDTA | 50 (mM) | |
| 5 | 1 | reservoir | ammonium sulfate | 2.4 (M) | |
| 6 | 1 | reservoir | dithiothreitol | 20 (mM) | |
| 7 | 1 | reservoir | Tris-HCl | 100 (mM) |
