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. Author manuscript; available in PMC: 2019 Nov 1.
Published in final edited form as: Nat Chem Biol. 2019 Apr 8;15(5):510–518. doi: 10.1038/s41589-019-0265-y

Figure 3. Dimerisation and putative negative cooperativity in McsB.

Figure 3

a, Ribbon diagram of the dimeric interface of McsB (subunit 1, yellow; subunit 2, gray). b, Native MS of R273E and WT McsB. Full native MS spectrum for WT McsB is shown in Supplementary Fig. 9. c, SEC-MALS of R273E and WT McsB. The UV spectra (thin line) were scaled to equal height. The experimental MW measured with MALS is represented with a bold line. Full-width SDS-PAGE fragments are shown in Supplementary Figure 12c and SDS-PAGE analysis of SEC input samples in Supplementary Figure 12d. d, Summary of SEC-MALS results for the dimerisation-deficient mutants (raw data in Supplementary Fig. 5f,g). Vertical axis is in logarithmic scale. e, Radioactive kinase assay of dimerisation-deficient mutants in the presence of 12.5 mM ATP. Representative Phosphorimager scan (top) and quantification of 3 experiments with independently purified protein batches (bottom) are shown. Uncropped scan is shown in Supplementary Figure 12e. Error bars indicate standard deviation. f, Distribution of thermal motion factors in the apo and AMP-PN-bound McsB dimer. B factors are reflected in colouring and in cartoon putty radius.