Fig. 4: dMP screening of cross-linking conditions on ADH, GLDH and 20 proteasome. | Nature Communications

Fig. 4: dMP screening of cross-linking conditions on ADH, GLDH and 20 proteasome.

From: Denaturing mass photometry for rapid optimization of chemical protein-protein cross-linking reactions

Fig. 4

a Effect of cross-linking reagent (size, flexibility) on oligomeric states stabilized, measured in dMP: presented results are probability densities (KD) of GLDH samples cross-linked with increasing molar ratios of PhoX, DSAU, DSBU, from measurement replicates (n = 3). b dMP-based quantitative results of XL condition screening for ADH, GLDH, and 20S proteasome complexes. Bar charts represent the dMP-calculated global inter-XL efficiency (mean ± SD) for each complex and XL condition (25/100/400:1 cross-linker:complex molar ratio), from measurement replicates (n = 3). Plain dots represent the complex stabilization factor for each complex and XL condition. The black dash line corresponds to the stabilization factor value of 1 indicating a complex abundance similar to the native sample. Source data are provided as a Source Data file.

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