5KU7
Crystal structure of the TIR domain from the Muscadinia rotundifolia disease resistance protein RPV1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
Synchrotron site | Australian Synchrotron |
Beamline | MX1 |
Temperature [K] | 80 |
Detector technology | CCD |
Collection date | 2014-04-03 |
Detector | ADSC QUANTUM 210r |
Wavelength(s) | 0.9537 |
Spacegroup name | P 2 21 21 |
Unit cell lengths | 41.855, 89.117, 113.858 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 35.947 - 2.300 |
R-factor | 0.1853 |
Rwork | 0.180 |
R-free | 0.23460 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4csr |
RMSD bond length | 0.008 |
RMSD bond angle | 1.030 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.947 | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.091 | 0.927 |
Number of reflections | 19672 | |
<I/σ(I)> | 19.6 | 2.2 |
Completeness [%] | 100.0 | 100 |
Redundancy | 7.2 | 7.4 |
CC(1/2) | 0.990 | 0.784 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 16% PEG3350, 0.1M Tris pH 8.5 and 2% Tacsimate |