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) |