6DM4
Crystal structure of the SH2 domain from RavO (Lpg1129) from Legionella pneumophila in complex with Homo sapiens Shc1 phospho-Tyr317 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-02-26 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97932 |
| Spacegroup name | P 1 |
| Unit cell lengths | 44.454, 45.035, 74.748 |
| Unit cell angles | 72.60, 90.14, 77.55 |
Refinement procedure
| Resolution | 14.815 - 1.900 |
| R-factor | 0.1847 |
| Rwork | 0.182 |
| R-free | 0.23010 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.616 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((dev_3092: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 1.950 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.050 | 0.572 |
| Rmeas | 0.062 | 0.696 |
| Rpim | 0.036 | 0.392 |
| Number of reflections | 41529 | 2095 |
| <I/σ(I)> | 33.19 | 3.22 |
| Completeness [%] | 96.9 | 96.6 |
| Redundancy | 3.1 | 3.1 |
| CC(1/2) | 0.864 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 298 | 0.2 mM pTyr317 Shc1 peptide, 0.2 M ammonium sulfate, 0.1 M Tris pH 8.5, 25% (w/v) PEG 5K MME |
