4C6S
Crystal structure of the TIR domain from the Arabidopsis Thaliana disease resistance protein RRS1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-07-29 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9537,1.3776 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 71.265, 71.265, 66.724 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.632 - 1.751 |
| R-factor | 0.1829 |
| Rwork | 0.182 |
| R-free | 0.19810 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | RPS4 TIR |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.067 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.2_1309) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 71.240 | 1.780 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.060 | 1.500 |
| Number of reflections | 17927 | |
| <I/σ(I)> | 32.3 | 1.7 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 14 | 11.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 1.8M AMMONIUM SULPHATE, 0.1M BIS-TRIS PH 7.0 |
