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@ARTICLE{Yokoyama:840627,
author = {Yokoyama, Takeshi and Ostermann, Andreas and Schrader,
Tobias E. and Mizuguchi, Mineyuki},
title = {{L}arge-scale crystallization and neutron crystallographic
analysis of {HSP}70 in complex with {ADP}},
journal = {Acta crystallographica / F},
volume = {73},
number = {10},
issn = {2053-230X},
address = {Oxford [u.a.]},
publisher = {Blackwell},
reportid = {FZJ-2017-08132},
pages = {555 - 559},
year = {2017},
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-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.},
cin = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
(München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
ddc = {530},
cid = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
I:(DE-Juel1)JCNS-1-20110106},
pnm = {6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
Neutron Research (JCNS) (POF3-623)},
pid = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4},
experiment = {EXP:(DE-MLZ)BIODIFF-20140101},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:28994403},
UT = {WOS:000412683100003},
doi = {10.1107/S2053230X1701264X},
url = {https://juser.fz-juelich.de/record/840627},
}