1GWB
STRUCTURE OF GLYCOPROTEIN 1B
Experimental procedure
| Experimental method | SINGLE WAVELENGTH | 
| Source type | SYNCHROTRON | 
| Source details | ESRF BEAMLINE ID14-4 | 
| Synchrotron site | ESRF | 
| Beamline | ID14-4 | 
| Temperature [K] | 100 | 
| Spacegroup name | P 64 2 2 | 
| Unit cell lengths | 202.000, 202.000, 128.000 | 
| Unit cell angles | 90.00, 90.00, 120.00 | 
Refinement procedure
| Resolution | 15.000 - 2.800 | 
| R-factor | 0.245 | 
| Rwork | 0.245 | 
| R-free | 0.27500  *  | 
| Structure solution method | MIR | 
| RMSD bond length | 0.008 | 
| RMSD bond angle | 1.840 | 
| Refinement software | CNS (1.1) | 
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | |
| High resolution limit [Å] | 2.800 | |
| Rmerge | 0.110  *  | 0.471 *  | 
| Number of reflections | 37462 | |
| <I/σ(I)> | 9.1 | |
| Completeness [%] | 99.8  *  | 99.8 *  | 
| Redundancy | 11.1  *  | 8.9 *  | 
Crystallization Conditions
| crystal ID | method | pH | temperature | details | 
| 1 | Vapor diffusion, sitting drop *  | 6.5 | 20 *  | pH 6.50 | 
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details | 
| 1 | 1 | drop | protein | 6-10 (mg/ml) | |
| 2 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH6.5 | 
| 3 | 1 | reservoir | ammonium sulfate | 2 (M) | 






