1G4B
CRYSTAL STRUCTURES OF THE HSLVU PEPTIDASE-ATPASE COMPLEX REVEAL AN ATP-DEPENDENT PROTEOLYSIS MECHANISM
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Spacegroup name | P 3 2 1 |
Unit cell lengths | 173.376, 173.376, 254.411 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 10.000 - 7.000 |
R-factor | 0.401 * |
Rwork | 0.401 |
R-free | 0.43200 |
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] | 80.000 * |
High resolution limit [Å] | 7.000 * |
Rmerge | 0.201 * |
Number of reflections | 6489 * |
Completeness [%] | 87.0 * |
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 | 27 (mg/ml) | |
2 | 1 | reservoir | MES | 0.1 (M) | |
3 | 1 | reservoir | 1.5 (M) | ||
4 | 1 | drop | Tris-HCl | 20 (mM) | |
5 | 1 | drop | 5 (mM) | ||
6 | 1 | drop | EDTA | 0.5 (mM) | |
7 | 1 | drop | dithiothreitol | 1 (mM) | |
8 | 1 | drop | glycerol | 10 (%) |