5AB0
Crystal structure of aminopeptidase ERAP2 with ligand
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALBA BEAMLINE XALOC |
| Synchrotron site | ALBA |
| Beamline | XALOC |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-11-30 |
| Detector | DECTRIS PILATUS 2M |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 75.350, 134.420, 129.000 |
| Unit cell angles | 90.00, 90.49, 90.00 |
Refinement procedure
| Resolution | 65.726 - 2.500 |
| R-factor | 0.201 |
| Rwork | 0.198 |
| R-free | 0.25800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4e36 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.282 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 65.700 | 2.640 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.110 | 0.810 |
| Number of reflections | 88335 | |
| <I/σ(I)> | 6 | 1.6 |
| Completeness [%] | 99.5 | 99.5 |
| Redundancy | 3.7 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.3 | 6 %(W/V) PEG MW 8000, 25 %(V/V) ETHYLENE GLYCOL, 59 MM MES AND 41 MM IMIDAZOLE AT PH 6.3 |
