6WYS
Lon protease proteolytic domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.3 |
| Synchrotron site | ALS |
| Beamline | 5.0.3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-06-22 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9765 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 187.789, 187.789, 158.411 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 72.341 - 2.229 |
| R-factor | 0.189 |
| Rwork | 0.188 |
| R-free | 0.21330 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2x36 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.853 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless (0.5.25) |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 93.890 | 93.890 | 2.300 |
| High resolution limit [Å] | 2.229 | 9.190 | 2.230 |
| Rmerge | 0.077 | 0.015 | 1.344 |
| Rmeas | 0.087 | 0.017 | 1.557 |
| Rpim | 0.041 | 0.008 | 0.775 |
| Total number of observations | 3544 | 17420 | |
| Number of reflections | 52150 | 801 | 4480 |
| <I/σ(I)> | 13.2 | 49.9 | 1 |
| Completeness [%] | 100.0 | 99.2 | 100 |
| Redundancy | 4.5 | 4.4 | 3.9 |
| CC(1/2) | 0.999 | 1.000 | 0.295 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 277 | 0.1M sodium chloride, 1.6M ammonium sulfate, 0.1M HEPES pH 7.5 |
