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Fig. 5 | BMC Biology

Fig. 5

From: Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control

Fig. 5

SGTA C-terminal domain is able to dimerise in the full-length context I. a Native mass spectrometry chromatograms of the SGTA FL protein (left) and the NT-TPR (upright) and FLΔQ (downright) constructs. Peaks corresponding to the same species are marked with colored circles with the charge number written inside. The theoretical molecular weight appears under the title and the obtained molecular weights for each species are shown on the right following the corresponding color. b SAXS analysis of SGTA FL (red) and NT-TPR (green) proteins: distance distribution plot (top left), Kratky plot (top right) and ensemble optimization method analysis data (bottom)

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