1FN4
CRYSTAL STRUCTURE OF FAB198, AN EFFICIENT PROTECTOR OF ACETYLCHOLINE RECEPTOR AGAINST MYASTHENOGENIC ANTIBODIES
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ELETTRA BEAMLINE 5.2R |
Synchrotron site | ELETTRA |
Beamline | 5.2R |
Temperature [K] | 100 |
Spacegroup name | I 41 2 2 |
Unit cell lengths | 169.780, 169.780, 182.570 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.800 |
R-factor | 0.198 |
Rwork | 0.198 |
R-free | 0.29400 |
RMSD bond length | 0.012 |
RMSD bond angle | 28.500 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.046 | 0.217 |
Total number of observations | 112032 * | |
Number of reflections | 32382 | |
Completeness [%] | 98.0 | 98.9 |
Redundancy | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.1 * | 18 * | 12 MG/ML FAB198, 1.6 M AS, 0.4 M CACL2, 0.1 M PB, 0.1% PEG 10000, PH 7.5, VAPOR DIFFUSION, SITTING DROP |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 12 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 1.6 (M) | |
3 | 1 | reservoir | 0.4 (M) | ||
4 | 1 | reservoir | phosphate | 0.1 (M) | pH8.1 |
5 | 1 | reservoir | PEG10000 | 0.1 (%) |