1G39
WILD-TYPE HNF-1ALPHA DIMERIZATION DOMAIN
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-2 |
| Synchrotron site | SSRL |
| Beamline | BL9-2 |
| Temperature [K] | 200 |
| Detector technology | CCD |
| Collection date | 2000-02-24 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 40.610, 37.330, 41.160 |
| Unit cell angles | 90.00, 90.04, 90.00 |
Refinement procedure
| Resolution | 20.600 - 1.220 |
| R-factor | 0.2552 |
| Rwork | 0.256 |
| R-free | 0.27800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | peptide model with selenomethionine substituted at position 12 solved by MAD |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.700 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.600 | 1.280 |
| High resolution limit [Å] | 1.220 | 1.220 |
| Rmerge | 0.051 | 0.497 * |
| Number of reflections | 36802 | |
| <I/σ(I)> | 24.6 | 2.2 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 5.3 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 8.5 | 277 | PEG 4000, Tris-HCl, lithium sulphate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | peptide | 10 (mg/ml) | |
| 2 | 1 | reservoir | PEG4000 | 24 (%) | |
| 3 | 1 | reservoir | Tris-HCl | 80 (mM) | |
| 4 | 1 | reservoir | 0.16 (M) |
