1Q88
Crystal structure of the C-domain of the T.vaginalis Inr binding protein, IBP39 (monoclinic form)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 298 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-12-10 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 99.600, 76.400, 80.300 |
| Unit cell angles | 90.00, 93.00, 90.00 |
Refinement procedure
| Resolution | 49.700 * - 2.420 |
| R-factor | 0.19 |
| Rwork | 0.190 |
| R-free | 0.23400 * |
| Structure solution method | MIR |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.500 * |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | CNS |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.700 | 2.500 |
| High resolution limit [Å] | 2.420 | 2.420 |
| Rmerge | 0.064 * | 0.245 * |
| Total number of observations | 62819 * | |
| Number of reflections | 18750 | |
| <I/σ(I)> | 15.2 | |
| Completeness [%] | 98.9 | 83 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 6.5 | 298 | PEG 5000, ammonium sulphate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20-50 (mg/ml) | |
| 2 | 1 | reservoir | ammonium sulfate | 200 (mM) | |
| 3 | 1 | reservoir | MES | 50 (mM) | pH6.5 |
| 4 | 1 | reservoir | PEG5000 | 15 (%) | |
| 5 | 1 | reservoir | sodium phosphate | 1 (M) | pH7.0 |
