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