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 |