1EKF
CRYSTALLOGRAPHIC STRUCTURE OF HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL) COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE AT 1.95 ANGSTROMS (ORTHORHOMBIC FORM)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.2 |
| Synchrotron site | ALS |
| Beamline | 5.0.2 |
| Temperature [K] | 223 |
| Detector technology | CCD |
| Collection date | 1999-04-20 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 69.385, 105.032, 107.016 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.290 - 1.950 |
| R-factor | 0.232 |
| Rwork | 0.222 |
| R-free | 0.26000 |
| Starting model (for MR) | E. COLI BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE. |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.584 * |
| 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] | 24.290 | 2.070 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.065 | 0.414 |
| Number of reflections | 48329 | |
| <I/σ(I)> | 21.34 | |
| Completeness [%] | 83.8 | 63.8 |
| Redundancy | 4.81 | 1.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | PEG1500, HEPES, DTT, pH 7.0, 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 | PEG1500 | 22-30 (%) | |
| 6 | 1 | reservoir | HEPES | 100 (mM) | |
| 7 | 1 | reservoir | dithiothreitol | 20 (mM) |
