3GS0
Human transthyretin (TTR) complexed with (S)-3-(9H-fluoren-9-ylideneaminooxy)-2-methylpropanoic acid (inhibitor 16)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 |
Temperature [K] | 120 |
Detector technology | IMAGE PLATE |
Collection date | 2007-02-02 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 43.390, 85.979, 65.076 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.370 - 1.850 |
R-factor | 0.23165 |
Rwork | 0.230 |
R-free | 0.26930 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bmz |
RMSD bond length | 0.023 |
RMSD bond angle | 2.227 |
Data reduction software | CrystalClear |
Data scaling software | CrystalClear |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.370 | 1.898 |
High resolution limit [Å] | 1.850 | 1.850 |
Number of reflections | 21224 | |
Completeness [%] | 98.7 | 97.45 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 290 | Crystals of wt-TTR were obtained from 5-7 mg/mL protein solutions (in 100 mM KCl, 1 mM EDTA, 10 mM sodium phosphate, pH 7.0, 0.3 M ammonium sulfate) equilibrated against 2 M ammonium sulfate in hanging drops. All TTR:ligand complexes were prepared from crystals soaked with a ten fold molar excess of ligand for more than three weeks., VAPOR DIFFUSION, HANGING DROP, temperature 290K |