1C5D
THE CRYSTAL STRUCTURE OF THE FAB FRAGMENT OF A RAT MONOCLONAL ANTIBODY AGAINST THE MAIN IMMUNOGENIC REGION OF THE HUMAN MUSCLE ACETYLCHOLINE RECEPTOR
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ELETTRA BEAMLINE 5.2R |
| Synchrotron site | ELETTRA |
| Beamline | 5.2R |
| Temperature [K] | 100 |
| Collection date | 1996-07-01 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 79.710, 110.080, 199.520 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.400 |
| R-factor | 0.196 |
| Rwork | 0.196 |
| R-free | 0.30400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2cgr |
| RMSD bond length | 0.010 |
| RMSD bond angle | 30.800 * |
| Data reduction software | AUTOMAR |
| Data scaling software | XDS |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.8) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.500 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.087 | 0.232 |
| Total number of observations | 118352 * | |
| Number of reflections | 26381 | |
| <I/σ(I)> | 25.45 | 9.12 |
| Completeness [%] | 76.1 | 51.9 |
| Redundancy | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 7.5 | 16 * | 12 MG/ML FAB192, 18% W/V PEG6000, 150 MM NACL, 100 MM BIS-TRIS/HCL, PH 7.5, 2 MM EDTA, AT 16 DEG. C, temperature 289K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 12 (mg/ml) | |
| 2 | 1 | reservoir | PEG6000 | 18 (%(w/v)) | |
| 3 | 1 | reservoir | 150 (mM) | ||
| 4 | 1 | reservoir | bis-Tris-HCl | 100 (mM) | |
| 5 | 1 | reservoir | EDTA | 2 (mM) |
