3CBR
Crystal structure of human Transthyretin (TTR) at pH3.5
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-BM-C |
| Synchrotron site | APS |
| Beamline | 14-BM-C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-07-24 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 43.124, 85.494, 62.419 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.580 - 1.700 |
| R-factor | 0.22472 |
| Rwork | 0.223 |
| R-free | 0.26048 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bmz |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.081 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | EPMR |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.580 | 1.650 |
| High resolution limit [Å] | 1.630 | 1.630 |
| Number of reflections | 29348 | |
| <I/σ(I)> | 19.36 | 2.69 |
| Completeness [%] | 98.2 | 88.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 3.5 | 289 | 5-7 mg/ml protein, 0.1 M sodium acetate, 20 % PEG 3350, 0.3-0.5 M ammonium sulfate equilibrated against 2.0M ammonium sulfate, pH 3.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
