2TRY
TERTIARY STRUCTURES OF THREE AMYLOIDOGENIC TRANSTHYRETIN VARIANTS AND IMPLICATIONS FOR AMYLOID FIBRIL FORMATION
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 296 |
Detector technology | IMAGE PLATE |
Collection date | 1995-12 |
Detector | RIGAKU |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 43.670, 86.370, 64.940 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 5.000 - 2.000 |
R-factor | 0.213 |
Rwork | 0.213 |
R-free | 0.31000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1tta |
RMSD bond length | 0.012 |
RMSD bond angle | 1.900 |
Data reduction software | bioteX |
Data scaling software | bioteX |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 64.900 | 2.000 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.107 | 0.270 |
Number of reflections | 17581 | |
<I/σ(I)> | 5 | 1.8 |
Completeness [%] | 74.9 | 56 |
Redundancy | 2.2 | 1.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | PURIFIED PROTEIN (25MG/ML IN 100MM TRIS BUFFER, PH 7.5) WAS CRYSTALLIZED FROM 1.5M AMMONIUM SULFATE, 100MM CITRATE BUFFER, PH 5.5, AT ROOM TEMPERATURE., pH 6.5 |