Journal Article

FZJ-2017-08132

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Large-scale crystallization and neutron crystallographic analysis of HSP70 in complex with ADP

Yokoyama, T. (Corresponding author) ; Ostermann, A. ; Schrader, T. E.FZJ* ; Mizuguchi, M.

2017
Blackwell Oxford [u.a.]

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Please use a persistent id in citations: http://hdl.handle.net/2128/16175  doi:10.1107/S2053230X1701264X

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.

Keyword(s): Health and Life (1st) ; Biology (2nd)

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Contributing Institute(s):

1. JCNS-FRM-II (JCNS (München) ; Jülich Centre for Neutron Science JCNS (München) ; JCNS-FRM-II)
2. Neutronenstreuung (Neutronenstreuung ; JCNS-1)

Research Program(s):

1. 6G15 - FRM II / MLZ (POF3-6G15) (POF3-6G15)
2. 6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623) (POF3-623)

Experiment(s):

1. BIODIFF: Diffractometer for large unit cells (NL1)

Appears in the scientific report 2017

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Database coverage:
; ; BIOSIS Previews ; Ebsco Academic Search ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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