1DUG
STRUCTURE OF THE FIBRINOGEN G CHAIN INTEGRIN BINDING AND FACTOR XIIIA CROSSLINKING SITES OBTAINED THROUGH CARRIER PROTEIN DRIVEN CRYSTALLIZATION
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X4A |
Synchrotron site | NSLS |
Beamline | X4A |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1997-03-15 |
Detector | FUJI |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 105.780, 105.780, 137.230 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.000 - 1.800 |
R-factor | 0.185 |
Rwork | 0.185 |
R-free | 0.22600 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.425 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.000 | 2.000 |
High resolution limit [Å] | 1.700 | 1.800 |
Rmerge | 0.054 | 0.250 |
Total number of observations | 376772 * | |
Number of reflections | 67736 | |
Completeness [%] | 89.2 | 66.1 |
Redundancy | 5.56 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | -170 * | PEG 3350, sodium acetate, sodium chloride, ammonium sulfate, Tris, reduced glutathione, pH 4.6, VAPOR DIFFUSION, HANGING DROP |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
10 | 1 | reservoir | ammonium sulfate | 35 (mM) | |
2 | 1 | drop | PEG3350 | 8 (%) | |
3 | 1 | drop | sodium acetate | 50 (mM) | |
4 | 1 | drop | sodium chloride | 25 (mM) | |
5 | 1 | drop | ammonium sulfate | 17.5 (mM) | |
6 | 1 | drop | Tris-HCl | 5 (mM) | |
7 | 1 | drop | glutathinoe | 5 (mM) | |
8 | 1 | reservoir | PEG3350 | 16 (%) | |
9 | 1 | reservoir | sodium acetate | 100 (mM) |