8GJF
afupcna bound with peptide mimetic
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-02-17 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9537 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 146.004, 84.830, 70.452 |
| Unit cell angles | 90.00, 91.41, 90.00 |
Refinement procedure
| Resolution | 42.200 - 2.000 |
| R-factor | 0.2345 |
| Rwork | 0.233 |
| R-free | 0.27030 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.196 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.18.2_3874) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.200 | 2.050 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.081 | 1.331 |
| Rmeas | 0.088 | 1.433 |
| Rpim | 0.033 | 0.527 |
| Total number of observations | 405868 | 30633 |
| Number of reflections | 57623 | 4252 |
| <I/σ(I)> | 13 | 1.6 |
| Completeness [%] | 99.2 | |
| Redundancy | 7 | 7.2 |
| CC(1/2) | 0.999 | 0.609 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 289 | 0.2 M Tacsimate pH 4.0, 0.1M Na Acetate, 16% PEG 3350 |
