2OR9
The structure of the anti-c-myc antibody 9E10 Fab fragment/epitope peptide complex reveals a novel binding mode dominated by the heavy chain hypervariable loops
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-08-25 |
Detector | MAR CCD 165 mm |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 76.068, 111.880, 134.119 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.700 |
Rwork | 0.252 |
R-free | 0.31000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1clo |
RMSD bond length | 0.008 |
RMSD bond angle | 1.410 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.800 |
High resolution limit [Å] | 2.700 | 2.700 |
Number of reflections | 31926 | |
<I/σ(I)> | 26.7 | 4.1 |
Completeness [%] | 99.5 | 97.4 |
Redundancy | 3.6 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 291 | 12% PEG 4000, 0.1 to 0.2 M sodium acetate, 0.02% sodium azide, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K |