7TAE
Crystal Structure of the NPR1-Interacting Domain of TGA3
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-11-24 |
Detector | DECTRIS EIGER2 X 16M |
Wavelength(s) | 0.9791 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 68.390, 101.740, 83.950 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.020 - 1.500 |
R-factor | 0.1897 |
Rwork | 0.189 |
R-free | 0.21070 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7tad |
RMSD bond length | 0.006 |
RMSD bond angle | 0.903 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.020 | 1.554 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.048 | |
Rmeas | 0.050 | |
Rpim | 0.014 | |
Number of reflections | 47111 | 4631 |
<I/σ(I)> | 25.51 | |
Completeness [%] | 99.8 | |
Redundancy | 13.2 | |
CC(1/2) | 0.999 | 0.947 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 10 mM HEPES (pH 8.0), 75 mM NaCl, 0.5 mM TCEP. 0.05 M sodium acetate pH 5.0, 10% (v/v) MPD 5 mg/mL protein |