Design and commissioning of a new synchrotron beamline dedicated to X-ray footprinting mass spectrometry

Gupta, S.; Russell, B.; Kristensen, L.G.; de Chant, J.; Lu, A.; Obst-Huebl, L.; Rad, B.; Tyler, J.; Subramanian, S.; Kidd, S.; Paul, S.; Chen, Y.; Petzold, C.J.; Kahan, D.N.; Costello, S.M.; Nakamura, K.; Inman, J.L.; MacDowell, A.A.; Spucces, A.; Ralston, C.Y.

doi:10.1107/S1600577526003711

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Figure 6
Single versus multiple exposure approach. (a) Bar plot showing ratio of % modification of amino acid residues at each exposure between the barstar–barnase complex and free barnase. (b) Bar plot generated by the % modification analysis showing either decrease (blue) or no change (gray) in solvent accessibility of amino acid residues in the barstar–barnase complex. The error bars show standard deviation for the dose rate replicates shown in Table S4. (c) Bar plot generated by XFMS dose-response analysis showing either a decrease (blue) or no change (gray) in solvent accessibility of amino acid residues when the barstar–barnase complex is formed. The error bars show the maximum and minimum values of the ratios shown in Table S3. (d) Residues of barnase highlighted with blue indicated >2-fold decrease in solvent accessibility upon complex formation. The structural model was generated by PDB 2za4 (Urakubo et al., 2008

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Volume 33| Part 4| July 2026|

https://doi.org/10.1107/S1600577526003711

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