1RTM
TRIMERIC STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN
Experimental procedure
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 80.000, 85.100, 98.500 |
| Unit cell angles | 90.00, 106.30, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.800 |
| R-factor | 0.22 |
| Rwork | 0.220 |
| R-free | 0.27000 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.300 |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 10.000 * |
| High resolution limit [Å] | 1.800 * |
| Rmerge | 0.044 * |
| Number of reflections | 54177 |
| Completeness [%] | 93.0 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 20 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | cl-MBP-A | 12 (mg/ml) | |
| 2 | 1 | drop | 10 (mM) | ||
| 3 | 1 | drop | 10 (mM) | ||
| 4 | 1 | reservoir | PEG3350 | 8-13 (%) | can be replaced with PEG8000 |
| 5 | 1 | reservoir | Tris-HCl | 100 (mM) | |
| 6 | 1 | reservoir | 20 (mM) | ||
| 7 | 1 | reservoir | 10 (mM) | ||
| 8 | 1 | reservoir | 0.02 (%) |
