2GAB
Human Transthyretin (TTR) Complexed with Hydroxylated polychlorinated Biphenyl-4-hydroxy-3,3',5,4'-tetrachlorobiphenyl
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 120 |
Detector technology | IMAGE PLATE |
Collection date | 1999-07-14 |
Detector | MAC Science DIP-2030 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 43.459, 86.197, 65.488 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 65.510 - 1.850 |
R-factor | 0.21147 |
Rwork | 0.210 |
R-free | 0.23769 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bmz |
RMSD bond length | 0.016 |
RMSD bond angle | 2.272 |
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] | 65.510 | 1.860 |
High resolution limit [Å] | 1.850 | 1.800 |
Rmerge | 0.030 | |
Number of reflections | 19133 | |
Completeness [%] | 89.2 | 92.35 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | CRYSTALLIZATION CONDITIONS: 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 , VAPOR DIFFUSION, HANGING DROP |