From the Cover: Direct protein interaction underlies gene-for-gene specificity and coevolution of the flax resistance genes and flax rust avirulence genes -- Dodds et al. 103 (23): 8888 Data Supplement - HTML Page - index.htslp -- Proceedings of the National Academy of Sciences

Dodds et al. 10.1073/pnas.0602577103.

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Fig. 4. Size exclusion chromatography of purified recombinant AvrL567-A, AvrL567-C, and AvrL567-D. After purification, AvrL567 protein samples were fractionated on Superdex 200 16/60 gel filtration column as described in Materials and Methods. The respective elution times of the major peaks of AvrL567-A, AvrL567-C and AvrL567-D at 258, 252, and 256 ml correspond to estimated molecular masses of 17, 15, and 16 kDa, based on the elution times of known molecular standards. This finding is consistent with a monomeric state of the proteins. AvrL567-A has an additional peak running in the void volume, suggesting a proportion of the protein forms large soluble aggregates. (Insets) The SDS/PAGE analysis of the fraction corresponding to the major peak (Post).