1IL0
X-RAY CRYSTAL STRUCTURE OF THE E170Q MUTANT OF HUMAN L-3-HYDROXYACYL-COA DEHYDROGENASE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-01-18 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 49.657, 87.719, 158.395 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.200 |
| R-factor | 0.219 |
| Rwork | 0.219 |
| R-free | 0.27600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1f0y |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.700 |
| Data reduction software | CrystalClear ((MSC/RIGAKU)) |
| Data scaling software | CrystalClear ((MSC/RIGAKU)) |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.090 | 0.264 |
| Number of reflections | 35973 | |
| <I/σ(I)> | 17.1 | 9.4 |
| Completeness [%] | 99.8 | 99.3 |
| Redundancy | 7.89 | 7.96 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 291 | Barycki, J.J., (1999) Biochemistry, 38, 5786. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5 (mg/ml) | |
| 2 | 1 | drop | NAD+ | 5 (mM) | |
| 3 | 1 | reservoir | N-[2-acetamido]-2-iminodiacetic acid | 50 (mM) | |
| 4 | 1 | reservoir | PEG4000 | 14-19 (%) |
