1G4A
CRYSTAL STRUCTURES OF THE HSLVU PEPTIDASE-ATPASE COMPLEX REVEAL AN ATP-DEPENDENT PROTEOLYSIS MECHANISM
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.3 |
| Synchrotron site | ALS |
| Beamline | 5.0.3 |
| Spacegroup name | P 3 2 1 |
| Unit cell lengths | 169.995, 169.995, 161.317 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 85.000 - 3.000 |
| R-factor | 0.2574 |
| Rwork | 0.257 |
| R-free | 0.29400 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.600 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 85.000 * |
| High resolution limit [Å] | 3.000 * |
| Rmerge | 0.131 * |
| Number of reflections | 46551 * |
| Completeness [%] | 86.0 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.8 * | dADP-HslU-HslV, VAPOR DIFFUSION |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 15 (mg/ml) | |
| 10 | 1 | reservoir | EDTA | 1 (mM) | |
| 2 | 1 | drop | Tris-HCl | 20 (mM) | |
| 3 | 1 | drop | 5 (mM) | ||
| 4 | 1 | drop | EDTA | 0.5 (mM) | |
| 5 | 1 | drop | dithiothreitol | 1 (mM) | |
| 6 | 1 | drop | glycerol | 10 (%) | |
| 7 | 1 | reservoir | ethylene glycol | 10 (%) | |
| 8 | 1 | reservoir | 20 (mM) | ||
| 9 | 1 | reservoir | dithiothreitol | 2 (mM) |
