1HX5
Crystal structure of M. tuberculosis chaperonin-10
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 298 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-11-15 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 77.500, 162.500, 125.600 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 3.500 |
| R-factor | 0.202 |
| Rwork | 0.202 |
| R-free | 0.26500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1lep |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 3.770 |
| High resolution limit [Å] | 3.500 | 3.500 |
| Rmerge | 0.078 | 0.280 |
| Number of reflections | 9927 | |
| <I/σ(I)> | 11.7 | |
| Completeness [%] | 96.4 | 90.5 |
| Redundancy | 7.7 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4 | 298 | PEG 400, lithium sulphate, sodium acetate, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 14 (mg/ml) | |
| 2 | 1 | drop | 10 (mM) | ||
| 3 | 1 | reservoir | PEG400 | 26 (%) | |
| 4 | 1 | reservoir | 210 (mM) | ||
| 5 | 1 | reservoir | acetate | 100 (mM) |
