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dc.contributor.authorVe, Thomas
dc.contributor.authorWilliams, Simon J
dc.contributor.authorStamp, Anna
dc.contributor.authorValkov, Eugene
dc.contributor.authorDodds, Peter N
dc.contributor.authorAnderson, Peter A
dc.contributor.authorKobe, Bostjan
dc.description.abstractThe 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 A˚ 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 P212121 and diffracted X-rays to 2.7 A˚ 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.
dc.publisherBlackwell Publishing
dc.relation.ispartofjournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
dc.subject.fieldofresearchMicrobiology not elsewhere classified
dc.titleCrystallization and X-ray diffraction analysis of the C-terminal domain of the flax rust effector protein AvrM
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorVe, Thomas

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