1BZD
TERTIARY STRUCTURES OF THREE AMYLOIDOGENIC TRANSTHYRETIN VARIANTS AND IMPLICATIONS FOR AMYLOID FIBRIL FORMATION
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 296 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-07-15 |
| Detector | RIGAKU RAXIS IIC |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 43.400, 86.120, 65.480 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 6.000 - 1.900 |
| R-factor | 0.188 |
| Rwork | 0.188 |
| R-free | 0.26500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1tsh |
| RMSD bond length | 0.011 |
| RMSD bond angle | 25.700 * |
| Data reduction software | bioteX |
| Data scaling software | bioteX |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 52.100 | 2.000 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.075 | 0.210 |
| Total number of observations | 146964 * | |
| Number of reflections | 19822 | |
| <I/σ(I)> | 7.2 | 1.6 |
| Completeness [%] | 67.8 | 49 |
| Redundancy | 2.6 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 5.5 | 23 * | PURIFIED PROTEIN (20MG/ML IN 25MM MONOBASIC SODIUM PHOSPHATE BUFFER, 0.15M NACL) WAS CRYSTALLIZED FROM 2M AMMONIUM SULFATE, 100MM CITRATE BUFFER, PH 5.5 AT ROOM TEMPERATURE. |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | drop | monobasic sodium phosphate | 25 (mM) | |
| 3 | 1 | drop | 0.15 (M) | ||
| 4 | 1 | reservoir | ammonium sulfate | 1.5-3 (M) | |
| 5 | 1 | reservoir | citrate | 100 (mM) |
