1JFU
CRYSTAL STRUCTURE OF THE SOLUBLE DOMAIN OF TLPA FROM BRADYRHIZOBIUM JAPONICUM
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-12-04 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 50.620, 75.150, 82.990 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 1.600 |
R-factor | 0.181 * |
Rwork | 0.181 |
R-free | 0.23400 |
Structure solution method | SIRAS |
RMSD bond length | 0.013 |
RMSD bond angle | 1.560 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHARP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 1.670 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.062 | 0.380 |
Number of reflections | 36890 | |
<I/σ(I)> | 16.2 | 2.5 |
Completeness [%] | 86.7 | 64 |
Redundancy | 3.5 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9 | 7 * | Bicine, NaCl, PEG550 MME, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 280K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | Bicine | 0.1 (M) | |
2 | 1 | reservoir | 0.1 (M) | ||
3 | 1 | reservoir | PEG550 MME | 30 (%) | |
4 | 1 | drop | protein | 16 (mg/ml) | in water |