2Z82
Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL41XU |
Synchrotron site | SPring-8 |
Beamline | BL41XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-04-10 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 84.650, 81.334, 90.904 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.680 - 2.600 |
R-factor | 0.215 |
Rwork | 0.215 |
R-free | 0.27700 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.500 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | CNS (1.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.760 |
High resolution limit [Å] | 2.600 | 2.600 |
Number of reflections | 18898 | |
Completeness [%] | 94.9 | 80.3 |
Redundancy | 5.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 296 | 0.2M ammonium sulfate, 0.1M Tris-HCl pH8.5 and 34% PEG1000, VAPOR DIFFUSION, HANGING DROP, temperature 296K |