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) |