5TDO
Crystal structure of the Fab fragment of anti-HER2 antibody 4D5 with redesigned heavy and light chain interfaces
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-07-15 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 1 |
| Unit cell lengths | 38.948, 79.953, 86.124 |
| Unit cell angles | 113.81, 93.02, 102.38 |
Refinement procedure
| Resolution | 24.071 - 1.610 |
| R-factor | 0.2382 |
| Rwork | 0.237 |
| R-free | 0.26710 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1fve |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.097 |
| Data reduction software | iMOSFLM (0.2.8) |
| Data scaling software | Aimless (0.2.8) |
| Phasing software | PHENIX (1.9_1692) |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 24.071 | 70.670 | 1.700 |
| High resolution limit [Å] | 1.610 | 5.090 | 1.610 |
| Rmerge | 0.052 | 0.046 | 0.372 |
| Rmeas | 0.074 | ||
| Rpim | 0.052 | ||
| Total number of observations | 225292 | ||
| Number of reflections | 113015 | ||
| <I/σ(I)> | 10.3 | ||
| Completeness [%] | 95.1 | 97.5 | 94 |
| Redundancy | 2 | 2 | 2 |
| CC(1/2) | 0.993 | 0.973 | 0.715 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 292 | 20% PEG3,350, 0.04 M Citrate, 0.06 M BTP, pH6.4 |
