3VRP
Crystal structure of the tyrosine kinase binding domain of Cbl-c in complex with phospho-EGFR peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44XU |
| Synchrotron site | SPring-8 |
| Beamline | BL44XU |
| Temperature [K] | 90 |
| Detector technology | CCD |
| Collection date | 2007-12-02 |
| Detector | Bruker DIP-6040 |
| Wavelength(s) | 0.900 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 93.357, 108.710, 54.936 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 33.780 - 1.520 |
| R-factor | 0.1789 |
| Rwork | 0.177 |
| R-free | 0.21000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.743 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (refmac_5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.550 |
| High resolution limit [Å] | 1.520 | 1.520 |
| Rmerge | 0.060 | 0.492 |
| Number of reflections | 43495 | |
| <I/σ(I)> | 33.698 | 4.16 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 5.7 | 5.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 10% PEG3350, 0.1M ammonium formate, 0.2M NDSB-201, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
