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024 7 _ |a 10.1107/S2053230X1701264X
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024 7 _ |a 2053-230X
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100 1 _ |a Yokoyama, Takeshi
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245 _ _ |a Large-scale crystallization and neutron crystallographic analysis of HSP70 in complex with ADP
260 _ _ |a Oxford [u.a.]
|c 2017
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520 _ _ |a HSP70 belongs to the heat-shock protein family and binds to unfolded proteins,driven by ATP hydrolysis, in order to prevent aggregation. Previous X-raycrystallographic analyses of HSP70 have shown that HSP70 binds to ADP withinternal water molecules. In order to elucidate the role of the water molecules,including their H/D atoms, a neutron diffraction study of the human HSP70ATPase domain was initiated. Deuterated large crystals of the HSP–ADPcomplex (1.2–1.8 mm3) were successfully grown by large-scale crystallization,and a neutron diffraction experiment at BIODIFF resulted in diffraction to amaximum resolution of 2.2 A ˚ . After data reduction, the overall completeness,Rmeas and average I/(I) were 90.4%, 11.7% and 8.1, respectively, indicating thatthe data set was sufficient to visualize H and D atoms.
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693 _ _ |a Forschungs-Neutronenquelle Heinz Maier-Leibnitz
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700 1 _ |a Ostermann, Andreas
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700 1 _ |a Schrader, Tobias E.
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700 1 _ |a Mizuguchi, Mineyuki
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773 _ _ |a 10.1107/S2053230X1701264X
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|t Acta crystallographica / F
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