9XRI
Crystal structure of MTH1 in complex with acoramidis bound at the active site and protein-protein interface (molar ratio 1:24)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-17A |
| Synchrotron site | Photon Factory |
| Beamline | BL-17A |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2025-10-19 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.950, 47.870, 124.250 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 37.920 - 1.080 |
| R-factor | 0.1569 |
| Rwork | 0.156 |
| R-free | 0.17280 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.898 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | EPMR |
| Refinement software | PHENIX ((1.21_5207: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.920 | 1.110 |
| High resolution limit [Å] | 1.080 | 1.080 |
| Rmeas | 0.091 | 0.687 |
| Number of reflections | 118172 | 8656 |
| <I/σ(I)> | 9.9 | 2.5 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 6.1 | 6.3 |
| CC(1/2) | 0.998 | 0.817 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | 1M sodium citrate, 0.2M sodium chloride, 0.1M cacodylate pH 6.5, 8mM acoramidis |
