Large-scale Crystallization and Neutron Crystallographic Analysis of HSP70 in Complex with ADP

Overview

Journal Acta Crystallogr F Struct Biol Commun

Specialty Chemistry

Date 2017 Oct 11

PMID 28994403

Citations 1

Authors

Takeshi Yokoyama

Andreas Ostermann

Tobias E Schrader

Mineyuki Mizuguchi

Affiliations

Soon will be listed here.

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 mm) 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, R 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.

Citing Articles

Neutron crystallographic analysis of the nucleotide-binding domain of Hsp72 in complex with ADP.

Yokoyama T, Fujii S, Ostermann A, Schrader T, Nabeshima Y, Mizuguchi M IUCrJ. 2022; 9(Pt 5):562-572.

PMID: 36071806 PMC: 9438496. DOI: 10.1107/S2052252522006297.

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