%0 Figure %A Mott, G. %A Thakur, Shalabh %A Smakowska, Elwira %A Wang, Pauline %A Belkhadir, Youssef %A Desveaux, Darrell %A Guttman, David %D 2016 %T Additional file 8: Figure S7. of Genomic screens identify a new phytobacterial microbe-associated molecular pattern and the cognate Arabidopsis receptor-like kinase that mediates its immune elicitation %U https://springernature.figshare.com/articles/figure/Additional_file_8_Figure_S7_of_Genomic_screens_identify_a_new_phytobacterial_microbe-associated_molecular_pattern_and_the_cognate_Arabidopsis_receptor-like_kinase_that_mediates_its_immune_elicitation/4456823 %R 10.6084/m9.figshare.c.3640832_D7.v1 %2 https://springernature.figshare.com/ndownloader/files/7186076 %K elicitation XPS 1 %K xup 25 peptide %K 0.111 μ M %K EC 50 %K PNG 20 kb %K EC 50 values %K Arabidopsis receptor-like kinase %K NT affinity analysis software %K ECD %K 0.381 μ M %K KD %K flg 22 binding data %K MST signal shift %K XPS 1 binding assays %K 13.13 μ M %X XPS1 binds specifically to xup25. Additional replicates of XPS1 binding assays. Titration of increasing amounts of xup25 peptide (a), but not flg22 (b), to a constant amount of XPS1 ECD (0.5 μM) induces a significant MST signal shift. At each peptide concentration a measurement was made using 60 % MST power and the values used to determine the KD or the EC50 with the NT affinity analysis software from Nanotemper. The KD fit plots are shown and both the KD and EC50 values are noted wherever possible. The calculated EC50 and KD values for xup25 were EC50 of 0.381 μM and KD of 0.111 μM. The flg22 binding data could not be fitted using the EC50 fit and has a KD of 13.13 μM. The standard error of the regression fit is 3.8404566 for (a) and 6.4503735 for (b). (PNG 20 kb) %I figshare