7PFS
Crystal structure of ERAP2 aminopeptidase in complex with phosphinic pseudotripeptide ((1R)-1-Amino-3-phenylpropyl){2-([1,1:3,1-terphenyl]-5-ylmethyl)-3-[((2S)-1-amino-1-oxo-3-phenylpropan-2-yl)-amino]-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 | 75.135, 133.822, 128.703 |
Unit cell angles | 90.00, 90.28, 90.00 |
Refinement procedure
Resolution | 65.030 - 2.700 |
R-factor | 0.1908 |
Rwork | 0.188 |
R-free | 0.23840 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5ab0 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.408 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX (1.14_3219) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 65.030 | 2.797 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.044 | |
Rpim | 0.044 | |
Number of reflections | 61923 | 3318 |
<I/σ(I)> | 10.76 | 1.72 |
Completeness [%] | 88.6 | |
Redundancy | 2 | |
CC(1/2) | 0.998 | 0.680 |
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 monosaccharide (0.2M D-glucose, 0.2M D-mannose, 0.2M D-galactose,0.2M L-fucose, 0.2M D-xylose, 0.2M N-acetyl-D-glucosamine), 0.1M MES/imidazole pH 6.5 |