6FAV
Crystal structure of C-terminal modified Tau peptide-hybrid 4.2f-I with 14-3-3sigma
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-09-30 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.977930 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 62.789, 70.140, 128.259 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.329 - 1.400 |
| R-factor | 0.1457 |
| Rwork | 0.144 |
| R-free | 0.17100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5hf3 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.908 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless (0.5.32) |
| Phasing software | PHASER (2.7.18) |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 47.330 | 47.330 | 1.420 |
| High resolution limit [Å] | 1.400 | 7.670 | 1.400 |
| Rmerge | 0.091 | 0.041 | 1.227 |
| Rmeas | 0.095 | 0.043 | 1.283 |
| Rpim | 0.027 | 0.012 | 0.370 |
| Total number of observations | 1357871 | 9956 | 65433 |
| Number of reflections | 112108 | 800 | 5529 |
| <I/σ(I)> | 14.3 | 43.3 | 2.2 |
| Completeness [%] | 100.0 | 99.8 | 100 |
| Redundancy | 12.1 | 12.4 | 11.8 |
| CC(1/2) | 0.999 | 0.999 | 0.621 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.1 | 277 | 26% PEG400, 10 mM HEPES pH 7.1, 5% glycerol, 0.19 M CaCl2 |
