%0 Journal Article
%A Yokoyama, Takeshi
%A Ostermann, Andreas
%A Schrader, Tobias E.
%A Mizuguchi, Mineyuki
%T Large-scale crystallization and neutron crystallographic analysis of HSP70 in complex with ADP
%J Acta crystallographica / F
%V 73
%N 10
%@ 2053-230X
%C Oxford [u.a.]
%I Blackwell
%M FZJ-2017-08132
%P 555 - 559
%D 2017
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:28994403
%U <Go to ISI:>//WOS:000412683100003
%R 10.1107/S2053230X1701264X
%U https://juser.fz-juelich.de/record/840627