6FAU
Crystal structure of C-terminal modified Tau peptide-hybrid 4.2e-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 PILATUS 6M |
| Wavelength(s) | 0.977930 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 62.800, 70.260, 128.180 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.350 - 1.250 |
| R-factor | 0.1457 |
| Rwork | 0.145 |
| R-free | 0.16420 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5hf3 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.833 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless (0.5.32) |
| Phasing software | PHASER (2.8.0) |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 47.350 | 47.350 | 1.270 |
| High resolution limit [Å] | 1.250 | 6.850 | 1.250 |
| Rmerge | 0.085 | 0.058 | 1.152 |
| Rmeas | 0.088 | 0.061 | 1.201 |
| Rpim | 0.025 | 0.017 | 0.337 |
| Total number of observations | 1915223 | ||
| Number of reflections | 157056 | 1105 | 7724 |
| <I/σ(I)> | 13.9 | ||
| Completeness [%] | 100.0 | 99.8 | 99.9 |
| Redundancy | 12.2 | 12.8 | 12.5 |
| CC(1/2) | 0.999 | 0.996 | 0.692 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 277 | 25% PEG400, 10 mM HEPES pH 7.1, 5% glycerol, 0.19 M CaCl2 |
