3D3L
The 2.6 A crystal structure of the lipoxygenase domain of human arachidonate 12-lipoxygenase, 12S-type
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2007-11-30 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 0.97627 |
| Spacegroup name | P 1 |
| Unit cell lengths | 59.590, 70.153, 77.868 |
| Unit cell angles | 65.37, 88.01, 69.82 |
Refinement procedure
| Resolution | 47.190 - 2.600 |
| R-factor | 0.20976 |
| Rwork | 0.206 |
| R-free | 0.27570 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1lox |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.309 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.193 | 2.740 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.158 | 0.509 |
| Number of reflections | 31408 | |
| <I/σ(I)> | 10.3 | 3.3 |
| Completeness [%] | 97.8 | 97.2 |
| Redundancy | 3.5 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4 | 293 | 1.0M LiCl2, 0.1M Citric acid pH 4.0, 20% PEG 6000, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
