8VCF
Crystal structure of Superbinder Src SH2 domain with Cysteine to Serine mutations
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2023-03-03 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.9794 |
| Spacegroup name | P 61 |
| Unit cell lengths | 67.481, 67.481, 46.886 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 33.740 - 1.500 |
| R-factor | 0.13853 |
| Rwork | 0.137 |
| R-free | 0.17664 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4f59 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.856 |
| Data reduction software | HKL-3000 |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0257) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.890 | 1.530 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.074 | 0.650 |
| Number of reflections | 19583 | 943 |
| <I/σ(I)> | 22.5 | 3.8 |
| Completeness [%] | 100.0 | 99.8 |
| Redundancy | 12.3 | 11.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 290 | VAPOR DIFFUSION,SITTING DROP, TEMPERATURE 290K 0.2 M Ammonium Fluoride, 20% PEG 3350 |
