8BN1
The structures of Ace2 in complex with bicyclic peptide inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I04-1 |
| Synchrotron site | Diamond |
| Beamline | I04-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-04-04 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 0.9179 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 193.253, 55.793, 122.843 |
| Unit cell angles | 90.00, 114.09, 90.00 |
Refinement procedure
| Resolution | 58.750 - 2.610 |
| R-factor | 0.25903 |
| Rwork | 0.255 |
| R-free | 0.32464 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1r42 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.309 |
| Data reduction software | DIALS |
| Data scaling software | xia2 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0352) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 112.230 | 112.230 | 2.660 |
| High resolution limit [Å] | 2.610 | 7.080 | 2.610 |
| Rmerge | 0.349 | 0.096 | 6.329 |
| Rmeas | 0.361 | 0.100 | 6.544 |
| Rpim | 0.092 | 0.026 | 1.650 |
| Total number of observations | 679243 | ||
| Number of reflections | 36877 | 1948 | 1850 |
| <I/σ(I)> | 5.5 | 30.4 | 0.3 |
| Completeness [%] | 100.0 | 100 | 100 |
| Redundancy | 15.6 | 14.3 | 15.8 |
| CC(1/2) | 0.996 | 0.997 | 0.329 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 25 %v/v PEGSH (Precipitant) 10 %v/v Glycerol (Precipitant) 0.2 M MgCl2 (Salt) 0.1 M TRIS 8 pH (Buffer) |
