| Products/Services Used | Details | Operation |
|---|---|---|
| Gene Synthesis | ... Macromolecule production The recombinant plasmid pET-22b(+)-HSPA1B ATPase domain (HSP70, residues 1–380) synthesized by GenScript was transformed into Escherichia coli BL21(DE3) cells (Table 1). HSP70A1A and HSP70A1B are collectively called HSP70 or ... | Get A Quote |
| Bacterial Expression System | Get A Quote |
HSP70 belongs to the heat-shock protein family and binds to unfolded proteins, driven by ATP hydrolysis, in order to prevent aggregation. Previous X-ray crystallographic analyses of HSP70 have shown that HSP70 binds to ADP with internal water molecules. In order to elucidate the role of the water molecules, including their H/D atoms, a neutron diffraction study of the human HSP70 ATPase domain was initiated. Deuterated large crystals of the HSP-ADP complex (1.2-1.8 mm3) were successfully grown by large-scale crystallization, and a neutron diffraction experiment at BIODIFF resulted in diffraction to a maximum resolution of 2.2 Å. After data reduction, the overall completeness, Rmeas and average I/σ(I) were... More
