1F86
TRANSTHYRETIN THR119MET PROTEIN STABILISATION
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-09-04 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 42.680, 85.770, 63.690 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 5.000 - 1.100 |
| R-factor | 0.138 * |
| Rwork | 0.147 |
| R-free | 0.17700 |
| Structure solution method | WILD-TYPE TTR (1TTA) |
| RMSD bond length | 0.015 |
| RMSD bond angle | 0.037 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.110 |
| High resolution limit [Å] | 1.100 | 1.100 |
| Rmerge | 0.048 | 0.497 |
| Total number of observations | 1561421 * | |
| Number of reflections | 95607 * | |
| <I/σ(I)> | 25.1 | |
| Completeness [%] | 98.4 | 95.3 |
| Redundancy | 16 | 7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 5.3 * | 277 | Damas, A.M., (1996) Acta Crystallog., D52, 966. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | ammonium sulfate | 41 (%) | |
| 3 | 1 | reservoir | sodium citrate | 200 (mM) |
