1LOX
RABBIT RETICULOCYTE 15-LIPOXYGENASE
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 93 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-08 |
| Detector | MARRESEARCH |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 198.900, 198.900, 136.100 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 16.000 - 2.400 |
| R-factor | 0.198 |
| Rwork | 0.198 |
| R-free | 0.24700 |
| Structure solution method | MIR |
| RMSD bond length | 0.010 |
| RMSD bond angle | 22.300 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASES |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.490 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.073 | 0.362 |
| Number of reflections | 39151 | |
| <I/σ(I)> | 9 | 2.3 |
| Completeness [%] | 97.9 | 95.7 |
| Redundancy | 4.33 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 | 25 * | PEG PH 7.5 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 90 (mg/ml) | |
| 2 | 1 | drop | inhibitor | 2-fold molar excess | |
| 3 | 1 | drop | 0.48 (M) | ||
| 4 | 1 | drop | HEPES | 50-200 (mM) | |
| 5 | 1 | drop | mPEG5000 | 0.5-2 (%) | |
| 6 | 1 | reservoir | 0.45 (M) | ||
| 7 | 1 | reservoir | HEPES | 100 (mM) | |
| 8 | 1 | reservoir | mPEG5000 | 1 (%) |
