1DL7
THE STRUCTURAL BASIS OF REPERTOIRE SHIFT IN AN IMMUNE RESPONSE TO PHOSPHOCHOLINE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 298 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 130.900, 35.900, 50.450 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.350 |
R-factor | 0.191 |
Rwork | 0.189 |
R-free | 0.26500 |
RMSD bond length | 0.014 |
RMSD bond angle | 1.900 |
Data reduction software | bioteX |
Data scaling software | bioteX |
Phasing software | EPMR |
Refinement software | TNT |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 10.000 | 2.420 |
High resolution limit [Å] | 2.350 | 2.350 |
Rmerge | 0.073 | 0.265 * |
Total number of observations | 47930 * | |
Number of reflections | 8983 | |
<I/σ(I)> | 8.5 | |
Completeness [%] | 84.0 | 47 * |
Redundancy | 2 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 6.5 | 298 | SODIUM/POTASSIUM PHOSPHATE, HEPES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5.6 (mg/ml) | |
2 | 1 | drop | NPPC | 2 (mM) | |
3 | 1 | reservoir | 1.5 (M) | ||
4 | 1 | reservoir | HEPES | 0.1 (M) |