1G1O
CRYSTAL STRUCTURE OF THE HIGHLY AMYLOIDOGENIC TRANSTHYRETIN MUTANT TTR G53S/E54D/L55S
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I711 |
Synchrotron site | MAX II |
Beamline | I711 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1998-06-05 |
Detector | MARRESEARCH |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 58.310, 58.310, 228.950 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 15.000 - 2.300 |
R-factor | 0.239 * |
Rwork | 0.238 |
R-free | 0.29000 |
RMSD bond length | 0.007 |
RMSD bond angle | 27.140 * |
Data reduction software | DENZO |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | X-PLOR |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.420 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.082 | 0.546 |
Total number of observations | 109159 * | |
Number of reflections | 20911 | 2960 * |
<I/σ(I)> | 8.8 | 1.3 |
Completeness [%] | 99.2 | 98.4 |
Redundancy | 5.2 | 5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 298 | PEG 5000 MME, sodium citrate, ammonium sulphate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 3 (mg/ml) | |
2 | 1 | drop | Tris | 50 (mM) | |
3 | 1 | reservoir | PEG MME5000 | 40-42 (%) | |
4 | 1 | reservoir | sodium citrate | 100 (mM) | |
5 | 1 | reservoir | ammonium sulfate | 100 (mM) |