1AD9
IGG-FAB FRAGMENT OF ENGINEERED HUMAN MONOCLONAL ANTIBODY CTM01
Experimental procedure
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX7.2 |
Synchrotron site | SRS |
Beamline | PX7.2 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1996-03 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 81.390, 104.630, 119.380 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 2.800 |
R-factor | 0.233 |
Rwork | 0.233 |
R-free | 0.28400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ad0 |
RMSD bond length | 0.008 |
RMSD bond angle | 27.600 * |
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 | 3.020 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.105 * | 0.377 * |
Total number of observations | 143861 * | |
Number of reflections | 25776 | |
<I/σ(I)> | 17.2 | 5.3 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 5.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6 * | 13-18% PEG4000/200-250MM LISO4, BUFFERED AT PH7.6 WITH 100MM 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 | 13-18 (%) | |
4 | 1 | reservoir | 200-250 (mM) | ||
5 | 1 | reservoir | Tris | 100 (mM) |