1DOV
CRYSTAL STRUCTURE OF THE ALPHA-CATENIN DIMERIZATION DOMAIN
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-1 |
Synchrotron site | SSRL |
Beamline | BL9-1 |
Temperature [K] | 288 |
Detector technology | IMAGE PLATE |
Collection date | 1997-11-25 |
Detector | MAR scanner 345 mm plate |
Spacegroup name | H 3 2 |
Unit cell lengths | 136.460, 136.460, 118.170 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 40.000 - 3.000 |
R-factor | 0.218 |
Rwork | 0.218 |
R-free | 0.26300 |
RMSD bond length | 0.008 |
RMSD bond angle | 14.600 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | DM |
Refinement software | CNS (0.5) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 3.160 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.082 | 0.322 |
Total number of observations | 33971 * | |
Number of reflections | 8574 | |
<I/σ(I)> | 11.6 | |
Completeness [%] | 99.6 | 100 |
Redundancy | 4 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.9 | 295 | PEG 400, Tris, urea, dithiothreitol, pH 8.9, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20-40 (mg/ml) | |
2 | 1 | reservoir | Tris-HCl | 200 (mM) | |
3 | 1 | reservoir | urea | 900 (mM) | |
4 | 1 | reservoir | PEG400 | 27 (%) | |
5 | 1 | reservoir | dithiothreitol | 10 (mM) |