Crystallization and X-ray diffraction analysis of the C-terminal domain of the flax rust effector protein AvrM

Thomas Ve, Simon Williams, Anna Stamp, Eugene Valkov, Peter Dodds, Peter Anderson, Bostjan Kobe

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    4 Citations (Scopus)


    The flax rust effector AvrM is a secreted protein of unknown fold that is recognized by the M resistance protein in flax. In order to investigate the structural basis of the AvrM-M interaction and possible virulence-associated functions of AvrM, the C-terminal domains of two different AvrM variants (AvrM-A and avrM) were crystallized. Crystals of native AvrM-A were obtained using pentaerythritol ethoxylate (15/4 EO/OH) as a precipitant and diffracted X-rays to 2.9 Å resolution. Selenomethionine-derivative crystals of similar quality were obtained using PEG 1500 as a precipitant. Both the native and selenomethionine-labelled AvrM-A crystals had symmetry of space group C2221 with eight molecules in the asymmetric unit. Crystals of avrM had symmetry of space group P2 12 12 1 and diffracted X-rays to 2.7 Å resolution. Initial AvrM-A phases were calculated using the single-wavelength anomalous dispersion (SAD) method and a partial model was built. Phases for avrM were obtained by molecular replacement using the partial AvrM-A model.

    Original languageEnglish
    Pages (from-to)1603-1607
    Number of pages5
    JournalActa Crystallographica Section F-Structural Biology and Crystallization Communications
    Issue number12
    Publication statusPublished - Dec 2011


    • AvrM
    • fungal effectors
    • plant disease resistance
    • single-wavelength anomalous dispersion


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