1IRA
COMPLEX OF THE INTERLEUKIN-1 RECEPTOR WITH THE INTERLEUKIN-1 RECEPTOR ANTAGONIST (IL1RA)
Experimental procedure
Source type | ROTATING ANODE |
Source details | MACSCIENCE M18X |
Temperature [K] | 296 |
Detector technology | AREA DETECTOR |
Collection date | 1994-09 |
Detector | SIEMENS |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 47.200, 84.600, 140.200 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.700 |
R-factor | 0.213 |
Rwork | 0.213 |
R-free | 0.31400 |
Structure solution method | MIR + MOLECULAR REPLACEMENT |
Starting model (for MR) | IL1RA STRUCTURE (PDB ENTRY 1ILR) AND TRUNCATED CD4 DOMAIN (PDB ENTRY 2CD4) |
RMSD bond length | 0.004 |
RMSD bond angle | 26.500 * |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | SQUASH |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 60.000 | 2.800 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.060 * | 0.325 * |
Total number of observations | 73407 * | |
Number of reflections | 15631 | |
Completeness [%] | 97.2 | 85.3 |
Redundancy | 4.7 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 8.8 * | 23 * | THE COMPLEX OF THE IL-1 RECEPTOR WITH THE ANTAGONIST WAS PREPARED BY MIXING A SOLUTION OF IL-1 RECEPTOR IN 50 MM TRIS (PH 7.5) AND 150 MM NACL WITH A SOLUTION OF IL1RA IN THE SAME BUFFER. THE COMPLEX WAS CRYSTALLIZED USING THE HANGING DROP METHOD. THE DROPS WERE PREPARED BY MIXING 4 UL OF THE PROTEIN SOLUTION WITH 1 UL OF RESERVOIR SOLUTION, CONTAINING 30% (W/V) PEG 3350, 400 MM MGCL2 IN 100 MM MOPS BUFFER (PH 7.0)., vapor diffusion - hanging drop |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 13 (mg/ml) | |
2 | 1 | reservoir | ammonium phosphate | 1.6 (M) |