Preliminary X-ray crystallographic study of staphylococcal -haemolysin monomer

Takaki Sugawara, Daichi Yamashita, Yoshikazu Tanaka, Jun Kaneko, Yoshiyuki Kamio, Isao Tanaka, Min Yao

    Research output: Contribution to journalArticlepeer-review

    3 Citations (Scopus)


    Staphylococcal -haemolysin is a β-barrel pore-forming toxin expressed by Staphylococcus aureus. -Haemolysin is secreted as a water-soluble monomeric protein which binds to target membranes and forms membrane-inserted heptameric pores. Although the crystal structures of the heptameric pore and monomer bound to an antibody have been determined, that of monomeric -haemolysin without binder has yet to be elucidated. Previous mutation studies showed that mutants of His35 retain the monomeric structure but are unable to assemble into heptamers. Here, -haemolysin H35A mutants were expressed, purified and crystallized. Diffraction data were collected to 2.90Å resolution. The crystals belonged to space group P61, with unit-cell parameters a = b = 151.3, c = 145.0Å. Molecular replacement found four molecules in an asymmetric unit. The relative orientation among molecules was distinct from that of the pore, indicating that the crystal contained monomeric -haemolysin.

    Original languageEnglish
    Pages (from-to)868-870
    Number of pages3
    JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
    Issue number8
    Publication statusPublished - 2013 Aug


    • monomer
    • pore-forming toxins
    • staphylococcal -haemolysin

    ASJC Scopus subject areas

    • Biophysics
    • Structural Biology
    • Biochemistry
    • Genetics
    • Condensed Matter Physics


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