TY  - JOUR
AU  - Yokoyama, Takeshi
AU  - Ostermann, Andreas
AU  - Schrader, Tobias E.
AU  - Mizuguchi, Mineyuki
TI  - Large-scale crystallization and neutron crystallographic analysis of HSP70 in complex with ADP
JO  - Acta crystallographica / F
VL  - 73
IS  - 10
SN  - 2053-230X
CY  - Oxford [u.a.]
PB  - Blackwell
M1  - FZJ-2017-08132
SP  - 555 - 559
PY  - 2017
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:28994403
UR  - <Go to ISI:>//WOS:000412683100003
DO  - DOI:10.1107/S2053230X1701264X
UR  - https://juser.fz-juelich.de/record/840627
ER  -