5X94
Crystal structure of SHP2_SH2-CagA EPIYA_D peptide complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-5A |
| Synchrotron site | Photon Factory |
| Beamline | BL-5A |
| Temperature [K] | 95 |
| Detector technology | CCD |
| Collection date | 2014-05-16 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 28.184, 121.968, 72.171 |
| Unit cell angles | 90.00, 101.26, 90.00 |
Refinement procedure
| Resolution | 70.781 - 2.600 |
| R-factor | 0.1632 |
| Rwork | 0.157 |
| R-free | 0.24590 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4dgp |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.051 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((1.10.1_2155)) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 70.800 |
| High resolution limit [Å] | 2.600 |
| Number of reflections | 28721 |
| <I/σ(I)> | 18.7 |
| Completeness [%] | 98.9 |
| Redundancy | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 31% PEG 4000, 0.1 M Tris-HCl |
