1QFP
N-TERMINAL DOMAIN OF SIALOADHESIN (MOUSE)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX7.2 |
| Synchrotron site | SRS |
| Beamline | PX7.2 |
| Temperature [K] | 287 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 38.900, 38.900, 152.500 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.800 |
| R-factor | 0.198 * |
| Rwork | 0.198 |
| R-free | 0.27600 |
| Structure solution method | MAD |
| RMSD bond length | 0.006 |
| RMSD bond angle | 25.700 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASES |
| Refinement software | CNS (0.5) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.970 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.067 | |
| Number of reflections | 3275 | |
| Completeness [%] | 89.7 | 89.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 5.6 * | 16 % (W/V) PEG 4000, 8% (V/V) PROPAN-2-OL, 10 MM DTT, 80MM SODIUM HEPES PH 7.5, 5MG/ML PROTEIN |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | 3' sialyllactose | 25 (mM) | |
| 3 | 1 | reservoir | PEG4000 | 30 (%(w/v)) | |
| 4 | 1 | reservoir | sodium citrate | 0.1 (M) | |
| 5 | 1 | reservoir | ammonium acetate | 0.2 (M) |






