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 |