9OMD
Crystal structure of Protease IV in complex with its propeptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08ID-1 |
| Synchrotron site | CLSI |
| Beamline | 08ID-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-04-08 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 0.953 |
| Spacegroup name | P 41 2 2 |
| Unit cell lengths | 192.120, 192.120, 231.840 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.410 - 3.300 |
| R-factor | 0.2627 |
| Rwork | 0.262 |
| R-free | 0.29110 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.473 |
| Data reduction software | autoPROC |
| Data scaling software | autoPROC |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.420 | 3.420 |
| High resolution limit [Å] | 3.300 | 3.300 |
| Rmerge | 0.191 | 1.328 |
| Rmeas | 0.195 | 1.352 |
| Rpim | 0.037 | 0.253 |
| Number of reflections | 65701 | 6463 |
| <I/σ(I)> | 19 | 3.6 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 26.9 | 28.4 |
| CC(1/2) | 0.999 | 0.898 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 295 | 100 mM MES pH 6.5, 5% MPD, 2.8 M ammonium sulfate |
