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 |
