2G5U
Human Transthyretin (TTR) Complexed with Hydroxylated polychlorinated Biphenyl-4,4'-dihydroxy-3,3',5,5'-tetrachlorobiphenyl
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 120 |
Detector technology | IMAGE PLATE |
Collection date | 1999-06-07 |
Detector | MAC Science DIP-2030 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 43.239, 85.841, 64.793 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 27.520 - 1.800 |
R-factor | 0.18199 |
Rwork | 0.180 |
R-free | 0.21972 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bmz |
RMSD bond length | 0.014 |
RMSD bond angle | 1.497 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 27.520 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.037 | |
Number of reflections | 21209 | |
Completeness [%] | 92.1 | 92.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | Crystals of recombinant WT TTR were obtained from protein solutions at 5 mg/ml (in 100 mM KCl, 100 mM phosphate [pH 7.4], 1 M ammonium sulfate) equilibrated against 2 M ammonium sulfate in hanging drop experiments. The TTR ligand complexes were prepared from crystals soaked for 2 weeks with a 10-fold molar excess , pH 7.00, VAPOR DIFFUSION, HANGING DROP, temperature 298K |