1G3I
CRYSTAL STRUCTURE OF THE HSLUV PROTEASE-CHAPERONE COMPLEX
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.2 |
| Synchrotron site | ALS |
| Beamline | 5.0.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-06-23 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.1 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 209.223, 220.579, 241.070 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.080 - 3.410 |
| R-factor | 0.24 |
| Rwork | 0.240 |
| R-free | 0.28400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | H. influenzae HslU at 2.3A H. influenzae HslV at 1.9A |
| RMSD bond length | 0.010 * |
| RMSD bond angle | 1.300 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 3.520 |
| High resolution limit [Å] | 3.400 | 3.400 |
| Rmerge | 0.064 | 0.285 |
| Total number of observations | 297864 * | |
| Number of reflections | 134912 | |
| <I/σ(I)> | 11.5 | 3 |
| Completeness [%] | 89.1 | 80.6 |
| Redundancy | 2.2 | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 * | 4 * | PEG monomethyl ether 2000, potassium Chloride, magnesium acetate, citrate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5-20 (mg/ml) | |
| 2 | 1 | drop | MOPS | 10 (mM) | |
| 3 | 1 | drop | 1 (mM) | ||
| 4 | 1 | drop | ATP | 1 (mM) | |
| 5 | 1 | reservoir | PEG2000MME | 3-6 (%) | |
| 6 | 1 | reservoir | 1 (M) | ||
| 7 | 1 | reservoir | 10 (mM) | ||
| 8 | 1 | reservoir | citrate | 50 (mM) |
