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000840627 1001_ $$00000-0002-5362-8606$$aYokoyama, Takeshi$$b0$$eCorresponding author
000840627 245__ $$aLarge-scale crystallization and neutron crystallographic analysis of HSP70 in complex with ADP
000840627 260__ $$aOxford [u.a.]$$bBlackwell$$c2017
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000840627 520__ $$aHSP70 belongs to the heat-shock protein family and binds to unfolded proteins,driven by ATP hydrolysis, in order to prevent aggregation. Previous X-raycrystallographic analyses of HSP70 have shown that HSP70 binds to ADP withinternal water molecules. In order to elucidate the role of the water molecules,including their H/D atoms, a neutron diffraction study of the human HSP70ATPase domain was initiated. Deuterated large crystals of the HSP–ADPcomplex (1.2–1.8 mm3) were successfully grown by large-scale crystallization,and a neutron diffraction experiment at BIODIFF resulted in diffraction to amaximum resolution of 2.2 A ˚ . After data reduction, the overall completeness,Rmeas and average I/(I) were 90.4%, 11.7% and 8.1, respectively, indicating thatthe data set was sufficient to visualize H and D atoms.
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000840627 7001_ $$0P:(DE-HGF)0$$aOstermann, Andreas$$b1
000840627 7001_ $$0P:(DE-Juel1)138266$$aSchrader, Tobias E.$$b2$$ufzj
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