5AB2
Crystal structure of aminopeptidase ERAP2 with ligand
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06DA |
| Synchrotron site | SLS |
| Beamline | X06DA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-02-08 |
| Detector | DECTRIS PILATUS 2M |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 75.650, 135.465, 128.212 |
| Unit cell angles | 90.00, 90.24, 90.00 |
Refinement procedure
| Resolution | 49.007 - 2.729 |
| R-factor | 0.226 |
| Rwork | 0.223 |
| R-free | 0.28590 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4e36 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.423 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.440 | 2.880 |
| High resolution limit [Å] | 2.730 | 2.730 |
| Rmerge | 0.090 | 0.770 |
| Number of reflections | 68594 | |
| <I/σ(I)> | 11.4 | 2 |
| Completeness [%] | 99.9 | 99.8 |
| Redundancy | 6.4 | 6.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.3 | 7 %(W/V) PEG MW 8000, 20 %(V/V) ETHYLENE GLYCOL, 59 MM MES AND 41 MM IMIDAZOLE AT PH 6.3 |
