2Z80
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 | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-07-10 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 54.269, 101.383, 59.586 |
Unit cell angles | 90.00, 99.82, 90.00 |
Refinement procedure
Resolution | 39.890 - 1.800 |
R-factor | 0.22 |
Rwork | 0.220 |
R-free | 0.25400 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 1.400 |
Data reduction software | MOSFLM |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | CNS (1.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.910 |
High resolution limit [Å] | 1.800 | 1.800 |
Number of reflections | 57446 | |
Completeness [%] | 97.7 | 89.6 |
Redundancy | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 296 | 0.1M Tris-HCl pH8.5, 28% PEG2000, VAPOR DIFFUSION, HANGING DROP, temperature 296K |