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![[Figure 2]](yt5100fig2mag.jpg)
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Figure 2
Aae Hfq monomers and oligomers, as assayed by cross-linking and mass spectrometry. MALDI-TOF spectra are shown for (a) native, untreated (non-cross-linked) Aae Hfq monomers, with an expected MW of 9482.9 Da based on the recombinant protein sequence (Supplementary Fig. S1), as well as (b) a chemically cross-linked Aae Hfq sample. As detailed in § ![[link]](../../../../../../logos/arrows/d_arr.gif) 2.2, cross-linking assays employed a gentle (`indirect') method, using formaldehyde as a cross-linking agent. The main peaks in the cross-linked sample correspond to hexamers and dodecamers, with expected MWs of 56 897.4 and 113 794.8 Da, respectively. The singly-charged molecular ion peaks, [M+H]1+, are accompanied by schematics (blue and orange balls) that indicate the anticipated architecture of the oligomeric states, alongside the MW of the peak as determined from the mass spectrum (cross-linked species are better characterized by a MW range, rather than a single value, because of variability in the number of cross-linker molecules that react). |
![[Figure 2]](yt5100fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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