4XFO
Structure of an amyloid-forming segment TAVVTN from human Transthyretin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-E |
Synchrotron site | APS |
Beamline | 24-ID-E |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2012-12-09 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.9792 |
Spacegroup name | P 1 |
Unit cell lengths | 4.750, 10.660, 16.390 |
Unit cell angles | 77.64, 87.81, 77.61 |
Refinement procedure
Resolution | 16.010 - 1.350 |
R-factor | 0.135 |
Rwork | 0.134 |
R-free | 0.14780 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.270 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 16.010 |
High resolution limit [Å] | 1.350 |
Number of reflections | 629 |
<I/σ(I)> | 6.93 |
Completeness [%] | 92.6 |
Redundancy | 21.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 298 | 0.2 M Ammonium sulfate, 0.1 M BIS-TRIS pH 5.5, 25% w/v Polyethylene glycol 3,350, 25% Glycerol |