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. Author manuscript; available in PMC: 2021 Jul 13.
Published in final edited form as: Biochem Soc Trans. 2021 Jun 30;49(3):1361–1374. doi: 10.1042/BST20201080

Figure 4. Single-particle cryo-EM analysis of E. coli mechanosensitive channel YnaI.

Figure 4.

(A) Single-particle cryo-EM density of YnaI in a closed state. (EMD-11557) determined using DIBMA as a detergent-free method. The EM density in the transmembrane domain was not completely resolved; the EM density of TM1 and TM2 are not clear. (B) Single-particle cryo-EM structure of YnaI determined using detergent LMNG with addition of fluoridated Fos-choline 8 (EMD-20862). The transmembrane helices within the transmembrane domain are well resolved, however, no native lipid molecules were seen. (C) Single-particle cryo-EM density of YnaI in the claimed open state (EMD-11560). The EM density of transmembrane domain is not resolved at all, although the soluble domain is. (D) Structural comparison between YnaI determined using DIBMA (PDB: 6ZYD, orange colored) and LMNG (PDB: 6URT, gray colored). The two structures are significantly different for the TM1 and TM2 paddle, although the other portion is very similar; this reflects the potential bias of the structure determined using DIBMA resulting from the poor EM density in the transmembrane domain.