8V04
High resolution TMPRSS2 structure following acylation by nafamostat
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-03-19 |
| Detector | DECTRIS EIGER2 X 16M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 58.757, 50.502, 64.578 |
| Unit cell angles | 90.00, 91.60, 90.00 |
Refinement procedure
| Resolution | 39.810 - 1.580 |
| R-factor | 0.15695 |
| Rwork | 0.156 |
| R-free | 0.18084 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.659 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER (2.8.3) |
| Refinement software | REFMAC (5.8.0352) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 40.000 | 40.000 | 1.610 |
| High resolution limit [Å] | 1.580 | 4.290 | 1.580 |
| Rmerge | 0.099 | 0.047 | 0.663 |
| Rmeas | 0.127 | 0.059 | 0.851 |
| Rpim | 0.079 | 0.035 | 0.528 |
| Total number of observations | 212101 | ||
| Number of reflections | 94364 | 4962 | 4557 |
| <I/σ(I)> | 8.7 | ||
| Completeness [%] | 92.8 | 97.8 | 91.6 |
| Redundancy | 2.2 | 2.4 | 2.2 |
| CC(1/2) | 0.988 | 0.994 | 0.625 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 291 | 3 uL hanging drop (2:1 protein:precipitant) grown over precipitant solution containing 25%PEG4000, 0.2M ammonium sulfate, and 0.1M sodium acetate pH 4.6. Protein (10 mg/mL) was in a buffer containing 25 mM Tris pH 8.0, 75 mM NaCl, and 2 mM CaCl2 |
