8SV7
The 1.53 Angstrom structure of human Tango2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2023-04-08 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 49.730, 49.960, 241.380 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.710 - 1.530 |
Rwork | 0.168 |
R-free | 0.19570 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 0.796 |
Data reduction software | XDS (V. 220110) |
Data scaling software | XDS (V. 220110) |
Phasing software | PHENIX ((1.20.1_4487: ???)) |
Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.710 | 1.570 |
High resolution limit [Å] | 1.530 | 1.530 |
Rmerge | 0.045 | 0.499 |
Rmeas | 0.049 | 0.525 |
Rpim | 0.130 | |
Number of reflections | 84855 | 4390 |
<I/σ(I)> | 28.14 | 3.97 |
Completeness [%] | 94.2 | 65.1 |
Redundancy | 13.6 | |
CC(1/2) | 1.000 | 0.967 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | Equal parts of protein solution 25 mg/ml and a precipitate cocktail consisting of 1.0 M Ammonium sulfate, 0.1 M BIS-TRIS pH 5.5, 1% w/v Polyethylene glycol 3,350 |