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Acta Crystallogr F Struct Biol Commun. 2017 Oct 1;73(Pt 10):555-559. doi: 10.1107/S2053230X1701264X. Epub 2017 Sep 23.

Large-scale crystallization and neutron crystallographic analysis of HSP70 in complex with ADP.

Author information

  • 1Faculty of Pharmaceutical Sciences, University of Toyama, 2630 Sugutani, Toyama 930-0914, Japan.
  • 2Heinz Maier-Leibnitz Zentrum (MLZ), Technische Universtät München, Lichtenbergstrasse 1, 85748 Garching, Germany.
  • 3Jülich Centre for Neutron Science (JCNS) at Heinz Maier-Leibnitz Zentrum (MLZ), Forschungszentrum Jülich GmbH, Lichtenbergstrasse 1, 85748 Garching, Germany.

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.

KEYWORDS:

HSP70; heat-shock proteins; large-scale crystallization; neutron protein crystallography

PMID:
28994403
DOI:
10.1107/S2053230X1701264X
[PubMed - in process]
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