9EHD
Crystal structure of N-SH2 domain of SHP2 bound to GAB1 tyrosine phosphorylated peptide (624-633) QVEpYLDLDLD
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.1 |
| Synchrotron site | ALS |
| Beamline | 8.2.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2021-05-19 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.0005 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 61.530, 61.530, 73.445 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 37.430 - 1.590 |
| R-factor | 0.2046 |
| Rwork | 0.201 |
| R-free | 0.24000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.278 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.21rc1_5015) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.430 | 1.630 |
| High resolution limit [Å] | 1.590 | 1.590 |
| Number of reflections | 19583 | 1369 |
| <I/σ(I)> | 15.98 | |
| Completeness [%] | 99.9 | 99.85 |
| Redundancy | 25.9 | 27.1 |
| CC(1/2) | 1.000 | 0.415 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 291 | 500 nL of 10 mg/mL SHP2 N-SH2 in 50 mM Bis-Tris pH 6.5, 50 mM NaCl, 1 mM TCEP, with GAB1 (QVEpYLDLDLD) 1:1.05 molar ratio; 500 nL of 6% v/v Tacsimate pH 6.0, 0.1 M MES monohydrate pH 6.0, and 25% w/v polyethylene glycol 4,000 |
