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. 2013 Apr 2;52(14):4020-3.
doi: 10.1002/anie.201210197. Epub 2013 Feb 28.

Studying 18 MDa virus assemblies with native mass spectrometry

Joost Snijder  1 , Rebecca J Rose, David Veesler, John E Johnson, Albert J R Heck
Affiliations

Studying 18 MDa virus assemblies with native mass spectrometry

Joost Snijder et al. Angew Chem Int Ed Engl. .

Erratum in

  • Angew Chem Int Ed Engl. 2014 Mar 17;53(12):3051
No abstract available

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Figures

Figure 1
Figure 1
Monitoring assembly of HK97 capsids with native ESI-MS. a) Assembly and maturation pathway of HK97. b) Free capsomers with penton signal in blue and hexon signal in red. c) Intact Prohead I particle. A well-resolved series of charge states is observed allowing the accurate mass calculation.
Figure 2
Figure 2
Incomplete desolvation is the limiting factor in attaining narrow peak width in native MS of protein complexes. Experimental peaks of hexons (a) and Prohead-1gp5 (b) are compared to theoretical peaks with widths defined by instrument resolution and the natural isotope distribution. The ‘incomplete desolvation limited’ curves are simulated to fit the experimental data (m/z positions of the peaks are fixed and defined by the experimentally determined mass, the width is fitted to the signal). The numbers in parentheses indicate the effective resolution (FWHM).
Figure 3
Figure 3
Theoretical upper mass limit of native MS studies of protein complexes as a function of effective resolution. Shown are the separation between subsequent charge states (black line, right-hand y-axis) and the calculated peak width as a function of molecular weight (colored lines, left-hand y-axis).
See this image and copyright information in PMC

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