Open AccessCrystallization and X‐ray diffraction analysis of the C‐terminal domain of the flax rust effector protein AvrM
Author(s) -
Ve Thomas,
Williams Simon J.,
Stamp Anna,
Valkov Eugene,
Dodds Peter N.,
Anderson Peter A.,
Kobe Bostjan
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111037675
Subject(s) - crystallization , crystallography , diffraction , molecular replacement , resolution (logic) , pentaerythritol , materials science , x ray crystallography , chemistry , crystal structure , physics , optics , organic chemistry , fire retardant , artificial intelligence , computer science , composite material
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 C 222 1 with eight molecules in the asymmetric unit. Crystals of avrM had symmetry of space group P 2 1 2 1 2 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.