9G8V
StmPr1, Stenotrophomonas maltophilia Protease 1, 36 kDa alkine serine protease
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1) |
| Synchrotron site | PETRA III, EMBL c/o DESY |
| Beamline | P13 (MX1) |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-09-20 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.968 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 60.385, 86.382, 131.573 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.541 - 1.637 |
| Rwork | 0.173 |
| R-free | 0.20880 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.869 |
| Data reduction software | autoPROC |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0425) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.541 | 1.665 |
| High resolution limit [Å] | 1.637 | 1.637 |
| Rmerge | 0.178 | 1.322 |
| Rmeas | 0.185 | |
| Rpim | 0.050 | 0.377 |
| Number of reflections | 42779 | 2107 |
| <I/σ(I)> | 1.38 | |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 13.4 | 13.2 |
| CC(1/2) | 0.997 | 0.869 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293.15 | 1.8 M ammonium sulfate 0.1 M Tris |






