4C6R
Crystal structure of the TIR domain from the Arabidopsis Thaliana disease resistance protein RPS4
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 | 2011-04-08 |
Detector | ADSC QUANTUM 315r |
Spacegroup name | P 1 |
Unit cell lengths | 33.925, 78.637, 80.668 |
Unit cell angles | 65.63, 78.64, 78.93 |
Refinement procedure
Resolution | 19.598 - 2.050 |
R-factor | 0.1883 |
Rwork | 0.186 |
R-free | 0.22980 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ozi |
RMSD bond length | 0.008 |
RMSD bond angle | 1.090 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.600 | 2.110 |
High resolution limit [Å] | 2.050 | 2.050 |
Rmerge | 0.060 | 0.240 |
Number of reflections | 43623 | |
<I/σ(I)> | 16.6 | 5.9 |
Completeness [%] | 94.0 | 75.3 |
Redundancy | 3.8 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | 23% (W/V) PEG 3350, 0.2 M AMMONIUM CITRATE (PH 6.5), 0.2 M SODIUM CHLORIDE |