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- Title
Large-scale crystallization and neutron crystallographic analysis of HSP70 in complex with ADP.
- Authors
Yokoyama, Takeshi; Ostermann, Andreas; Schrader, Tobias E.; Mizuguchi, Mineyuki
- Abstract
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 90.4%, 11.7% and 8.1, respectively, indicating that the data set was sufficient to visualize H and D atoms.
- Subjects
HSP70 heat-shock proteins; PROTEIN crystallography; ADENOSINE diphosphate
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2017, Vol 73, Issue 10, p555
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X1701264X