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The A component (SmhA) of a tripartite pore-forming toxin from Serratia marcescens : expression, purification and crystallographic analysis
DOI:
10.1107/S2053230X20013862
Authors:
Alicia M.
Churchill-angus
(The University of Sheffield)
,
Svetlana E.
Sedelnikova
(The University of Sheffield)
,
Thomas H. B.
Schofield
(The University of Sheffield; University of Leeds)
,
Patrick J.
Baker
(The University of Sheffield)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Acta Crystallographica Section F Structural Biology Communications
, VOL 76
, PAGES 577 - 582
State:
Published (Approved)
Published:
December 2020
Diamond Proposal Number(s):
17773

Abstract: Tripartite α-pore-forming toxins are constructed of three proteins (A, B and C) and are found in many bacterial pathogens. While structures of the B and C components from Gram-negative bacteria have been described, the structure of the A component of a Gram-negative α-pore-forming toxin has so far proved elusive. SmhA, the A component from the opportunistic human pathogen Serratia marcescens, has been cloned, overexpressed and purified. Crystals were grown of selenomethionine-derivatized protein and anomalous data were collected. Phases were calculated and an initial electron-density map was produced.
Journal Keywords: pore-forming toxin; crystallization; ClyA family; Serratia
Subject Areas:
Biology and Bio-materials
Instruments:
I03-Macromolecular Crystallography
Documents:
ow5025.pdf