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. Author manuscript; available in PMC: 2019 Aug 7.
Published in final edited form as: Structure. 2018 Jul 5;26(8):1116–1126.e4. doi: 10.1016/j.str.2018.05.015

Figure 2. Three dimensional negative stain-EM reconstructions of representative oligomers from peptide insertion variants of Hsp16.5:

Figure 2.

24-subunit (WT-like), 30-subunit, 36-subunit, and 48-subunit (P1-like). The top panel shows a surface representation and the middle panel is a clipped view revealing internal structure. Unlike the 36-subunit oligomer, the internal anatomy of the intermediate 30 subunit class structure lacks density. However, the circumference for these two types of particles is similar. In contrast to the well-ordered arrangement of the 24- and 48-subunit oligomers, the intermediate size oligomers demonstrate enhanced heterogeneity and lack of symmetry. The relative particle distribution for each variant is given in Table 1. The bottom panel correlates the EM analysis with the BN-PAGE results (in cartoon representation) of the oligomer distribution and identifies the predominant species for P1 variants. (See also Figure S3)