2G9K
Human Transthyretin (TTR) Complexed with Hydroxylated polychlorinated Biphenyl-4-hydroxy-2',3,3',4',5-Pentachlorobiphenyl
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 120 |
Detector technology | IMAGE PLATE |
Collection date | 1999-07-31 |
Detector | MAC Science DIP-2030 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 43.081, 85.461, 64.237 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 27.420 - 1.850 |
R-factor | 0.21586 |
Rwork | 0.214 |
R-free | 0.25745 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bmz |
RMSD bond length | 0.011 |
RMSD bond angle | 1.496 |
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] | 27.420 | 1.898 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.036 | |
Number of reflections | 18746 | |
Completeness [%] | 90.5 | 87.52 |
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 |