1CGD
HYDRATION STRUCTURE OF A COLLAGEN PEPTIDE
Experimental procedure
| Detector technology | DIFFRACTOMETER |
| Detector | ENRAF-NONIUS FAST |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 173.460, 14.057, 25.308 |
| Unit cell angles | 90.00, 95.82, 90.00 |
Refinement procedure
| Resolution | 12.500 - 1.850 |
| R-factor | 0.172 |
| Rwork | 0.172 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.530 |
| Data reduction software | MOLEN |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 86.700 |
| High resolution limit [Å] | 1.850 |
| Number of reflections | 5595 |
| Completeness [%] | 99.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 4 * | Bella, J., (1994) Science, 266, 75. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | peptide | 4.0-6.0 (mg/ml) | |
| 2 | 1 | drop | acetic acid | 10 (%) | |
| 3 | 1 | drop | PEG400 | 9.5 (%) | |
| 4 | 1 | drop | sodium azide | 0.1 (%) | |
| 5 | 1 | reservoir | PEG400 | 19 (%) |
