1HIB
THE STRUCTURE OF AN INTERLEUKIN-1 BETA MUTANT WITH REDUCED BIOACTIVITY SHOWS MULTIPLE SUBTLE CHANGES IN CONFORMATION THAT AFFECT PROTEIN-PROTEIN RECOGNITION
Experimental procedure
Spacegroup name | P 65 2 2 |
Unit cell lengths | 55.430, 55.430, 241.940 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 10.000 - 2.400 |
R-factor | 0.19 |
Rwork | 0.190 |
RMSD bond length | 0.017 |
RMSD bond angle | 0.046 * |
Phasing software | X-PLOR |
Refinement software | PROLSQ |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 9999.000 * |
High resolution limit [Å] | 2.270 * |
Rmerge | 0.062 * |
Total number of observations | 30094 * |
Number of reflections | 8534 * |
Completeness [%] | 90.0 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 3.4 (mg/ml) | |
2 | 1 | drop | ammonium sulfate | 0.168 (M) | |
3 | 1 | reservoir | ammonium sulfate | 2.1 (M) |