1S78
Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.1 |
| Synchrotron site | ALS |
| Beamline | 5.0.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-11-19 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 139.412, 139.412, 356.873 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 15.000 - 3.250 |
| R-factor | 0.22655 |
| Rwork | 0.224 |
| R-free | 0.26772 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Rat ErbB2 extracellular domain (PDB code 1N8Y) and uncomplexed pertuzumab Fab (PDB code 1L7I) |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.273 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 3.370 |
| High resolution limit [Å] | 3.250 | 3.250 |
| Rmerge | 0.116 | 0.691 |
| Number of reflections | 56351 | |
| <I/σ(I)> | 19.3 | 3.3 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 8.2 | 8.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | PEG 3350, ammonium formate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
