4UV7
The complex structure of extracellular domain of EGFR and GC1118A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B1 |
| Temperature [K] | 95 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 78.389, 84.172, 97.793 |
| Unit cell angles | 90.00, 97.11, 90.00 |
Refinement procedure
| Resolution | 19.750 - 2.100 |
| R-factor | 0.20429 |
| Rwork | 0.202 |
| R-free | 0.24759 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1yy9 |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.535 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.900 |
| High resolution limit [Å] | 1.900 | 1.870 |
| Rmerge | 0.090 | 0.940 |
| Number of reflections | 104241 | |
| <I/σ(I)> | 19.38 | 1.2 |
| Completeness [%] | 98.1 | 84.6 |
| Redundancy | 6.9 | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
