5TEC
Crystal structure of the TIR domain from the Arabidopsis thaliana NLR protein SNC1
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 | 2012-10-09 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9537 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 82.175, 82.175, 124.114 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.678 - 2.200 |
R-factor | 0.1801 |
Rwork | 0.178 |
R-free | 0.21680 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ozi |
RMSD bond length | 0.013 |
RMSD bond angle | 1.286 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHENIX |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 19.680 |
High resolution limit [Å] | 2.200 |
Number of reflections | 22223 |
<I/σ(I)> | 17.8 |
Completeness [%] | 99.8 |
Redundancy | 16.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 18%(w/v) PEG 3350, 9%(w/v) glycerol, 0.1 M MMT buffer pH 7.5 |