1ITB
TYPE-1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH INTERLEUKIN-1 BETA
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1995-07 |
Detector | RIGAKU |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 146.952, 68.452, 65.867 |
Unit cell angles | 90.00, 108.95, 90.00 |
Refinement procedure
Resolution | 15.000 - 2.500 |
R-factor | 0.229 |
Rwork | 0.229 |
R-free | 0.32500 |
Structure solution method | MIR |
RMSD bond length | 0.012 |
RMSD bond angle | 26.200 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.050 | 0.104 |
Number of reflections | 20723 | |
<I/σ(I)> | 28 | 10.9 |
Completeness [%] | 96.4 | 94.9 |
Redundancy | 6.4 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 0-4 * | PROTEIN WAS CRYSTALLIZED BY HANGING DROP DIFFUSION AGAINST 2.8M AMMONIUM SULFATE, 100MM MES PH 6.0, vapor diffusion - hanging drop |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | ammonium salfate | 1.8 (M) | |
2 | 1 | reservoir | MES | 100 (mM) |