2XKN
Crystal structure of the Fab fragment of the anti-EGFR antibody 7A7
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 90 |
| Detector technology | CCD |
| Collection date | 2007-05-16 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 169.034, 57.327, 121.023 |
| Unit cell angles | 90.00, 122.51, 90.00 |
Refinement procedure
| Resolution | 22.614 - 1.400 |
| R-factor | 0.1454 |
| Rwork | 0.144 |
| R-free | 0.17650 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1hil |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.247 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 23.000 | 1.420 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.060 | 0.360 |
| Number of reflections | 191075 | |
| <I/σ(I)> | 13.1 | 3.1 |
| Completeness [%] | 99.6 | 98.9 |
| Redundancy | 4.5 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 15% PEG 8000, 100 MM TRISAC BUFFER PH 9.0, 10 MM EDTA FROM THE HAMPTON ADDITIVE SCREEN |
