6FFT
Neutron structure of human transthyretin (TTR) S52P mutant in complex with tafamidis at room temperature to 2A resolution (quasi-Laue)
Experimental procedure
| Experimental method | LAUE |
| Source type | NUCLEAR REACTOR |
| Source details | ILL BEAMLINE LADI III |
| Synchrotron site | ILL |
| Beamline | LADI III |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Collection date | 2017-03-01 |
| Detector | LADI III |
| Wavelength(s) | 2.7-3.6 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 43.901, 85.703, 65.540 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.866 - 2.000 |
| R-factor | 0.2363 |
| Rwork | 0.231 |
| R-free | 0.28010 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5clx |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.975 |
| Data reduction software | LAUEGEN |
| Data scaling software | LSCALE |
| Phasing software | REFMAC |
| Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.900 | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.121 | 0.208 |
| Rpim | 0.070 | 0.151 |
| Number of reflections | 17225 | 1364 |
| <I/σ(I)> | 6 | 4 |
| Completeness [%] | 71.9 | 56.3 |
| Redundancy | 2.6 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 2.3M sodium malonate pD 5.9 | |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 2.3M sodium malonate pD 5.9 |






