1Q89
Crystal structure of the C-domain of the T.vaginalis Inr binding protein, IBP39 (cubic crystal form)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 2001-12-10 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | I 2 3 |
Unit cell lengths | 108.750, 108.750, 108.750 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 76.500 - 2.750 |
R-factor | 0.197 |
Rwork | 0.197 |
R-free | 0.26400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1q88 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.190 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | MOLREP |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 76.500 | 2.820 |
High resolution limit [Å] | 2.750 | 2.750 |
Rmerge | 0.074 | 0.246 * |
Total number of observations | 35034 * | |
Number of reflections | 6272 | |
Completeness [%] | 94.0 | 89 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 6.5 | 298 | PEG 5000, ammonium sulphate, pH 6.5, VAPOR DIFFUSION, SITTING 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 | 25 (%) |