1AE6
IGG-FAB FRAGMENT OF MOUSE MONOCLONAL ANTIBODY CTM01
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX7.2 |
| Synchrotron site | SRS |
| Beamline | PX7.2 |
| Temperature [K] | 290 |
| Detector technology | IMAGE PLATE |
| Collection date | 1995-02 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 54.300, 66.550, 61.350 |
| Unit cell angles | 90.00, 103.40, 90.00 |
Refinement procedure
| Resolution | 15.000 - 3.000 |
| R-factor | 0.21 |
| Rwork | 0.210 |
| R-free | 0.31100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1AD9 - STRUCTURE OF THE ENGINEERED HUMAN CONSTRUCT OF CTM01 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 27.800 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR (3.851) |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 3.230 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.138 * | 0.252 * |
| Total number of observations | 15707 * | |
| Number of reflections | 7862 | |
| <I/σ(I)> | 5 | 2.1 |
| Completeness [%] | 91.1 | 88.3 |
| Redundancy | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6 * | 20-25% PEG4000, BUFFERED AT PH 5.6 WITH 20MM BIS-TRIS. |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | bis-Tris | 20 (mM) | |
| 2 | 1 | drop | protein | 10 (mg/ml) | |
| 3 | 1 | reservoir | PEG4000 | 20-25 (%) | |
| 4 | 1 | reservoir | Bis-Tris | 20 (mM) |






