TRPV1チャネルの構造解析をクライオ電子顕微鏡単粒子解析法で行い（Liao et al. Nature 2013 504:107）話題となったYifan Cheng博士（USCF, USA） にセミナーをお願いしました。

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  As a versatile tool in structural biology, single particle electron cryo-microscopy (cryo-EM) has been used to determine the three-dimensional (3D) structures of proteins and macromolecular complexes without the need for crystals. Recent technological breakthroughs in electron detector technologies have enabled developments of novel techniques in both data acquisition and image processing. Together, these novel technologies revolutionized single particle cryo-EM and enabled near atomic resolution structure determinations of a broad range of proteins complexes without the need of crystals. Thus, it is now feasible to use single particle cryo-EM to determine structures of protein complexes that are challenging for the more traditional X-ray crystallographic structure determination approach. This is particularly true for integral membrane proteins.
  The Transient Receptor Potential (TRP) ion channel is a large and functionally diverse superfamily, second only to potassium channels.
 TRPV1 is the founding member of a subfamily of thermosensitive TRP channels. Up to date, there is no crystal structure of any member of TRP channel family. Facilitated by novel single particle cryo-EM technology, we determined atomic structures of TRPV1 ion channels in three different conformations, ligand free apo state and in complexes with vanilloid agonist capsaicin, or resiniferatoxin and Double-Knot toxin. These structures revealed the atomic structure of TRPV1 ion channel, providing a structural blueprint for understanding unique aspects of TRP channel function. They also revealed the gating mechanism different from that of voltage gated ion channels.

Reference:Structure of the TRPV1 ion channel determined by electron cryo-microscopy.
Liao M1, Cao E, Julius D, Cheng Y.
Nature. 2013 Dec 5;504(7478):107-12. doi: 10.1038/nature12822.