7P7P
Crystal structure of ERAP2 aminopeptidase in complex with phosphinic pseudotripeptide((1R)-1-Amino-3-phenylpropyl){(2S)-3-[((2S)-1-amino-1-oxo-3-phenylpropan-2-yl)amino]-2-{[3-(2-hydroxyphenyl)-isoxazol-5-yl]methyl}-3-oxopropyl}phosphinic acid
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1) |
| Synchrotron site | PETRA III, EMBL c/o DESY |
| Beamline | P13 (MX1) |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-08-12 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.9763 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 75.342, 134.618, 129.137 |
| Unit cell angles | 90.00, 90.48, 90.00 |
Refinement procedure
| Resolution | 50.190 - 3.000 |
| R-factor | 0.1822 |
| Rwork | 0.180 |
| R-free | 0.23050 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5ab0 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.367 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.17.1_3660) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.190 | 3.107 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.057 | 0.429 |
| Number of reflections | 48793 | 2984 |
| <I/σ(I)> | 10.98 | 1.46 |
| Completeness [%] | 94.5 | |
| Redundancy | 2 | |
| CC(1/2) | 0.997 | 0.607 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277.15 | 10% w/v PEG 8000, 20% v/v ethylene glycol, 0.02M of each alcohol (0.2M 1,6-hexanediol, 0.2M 1-butanol, 0.2M (RS)-1,2-propanediol, 0.2M 2-propanol, 0.2M 1,4-butanediol, 0.2M 1,3-propanediol), 0.1M MES/imidazole pH 6.5 |
