8VJU
Structure of Human Neurolysin in complex with dynorphin A13 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-06-13 |
| Detector | DECTRIS EIGER2 S 16M |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 142.067, 60.257, 95.553 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 79.290 - 1.990 |
| R-factor | 0.1962 |
| Rwork | 0.195 |
| R-free | 0.21840 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond angle | 14.818 |
| Data reduction software | XDS |
| Data scaling software | STARANISO |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 79.290 | 2.111 |
| High resolution limit [Å] | 1.987 | 1.987 |
| Rmerge | 0.055 | 0.823 |
| Rmeas | 0.067 | 0.981 |
| Rpim | 0.037 | 0.528 |
| Total number of observations | 7684 | |
| Number of reflections | 48708 | 2435 |
| <I/σ(I)> | 9.7 | 1.4 |
| Completeness [%] | 84.9 | |
| Redundancy | 3 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 295 | 17.5 ~ 30 % polyethylene glycol 3,350 and 50 ~ 125 mM Bis-Tris HCl buffer, pH 6.5 |
