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and stability of thin, cryo-EM specimens. Biophys. J. 110:749–755.
Goehring, A., Lee, C.-H., Wang, K.H., Michel, J.C., Claxton, D.P., Baconguis, I., Althoff, T., Fischer, S., Garcia, C.,
Gouaux, E. (2014) Screening and large-scale expression of membrane proteins in mammalian cells for structural
studies. Nat. Protoc. 9:2574–2585.
Gohon, Y. (2002) Etude structurale et fonctionnelle de deux protéines membranaires, la bactériorhodopsine et le
récepteur nicotinique de l'acétylcholine, maintenues en solution aqueuse non détergente par des polymères
amphiphiles. Université Paris-VI, Paris, 467 p.
Gohon, Y., Dahmane, T., Ruigrok, R., Schuck, P., Charvolin, D., Rappaport, F., Timmins, P., Engelman, D.M., Tribet,
C., Popot, J.-L., Ebel, C. (2008) Bacteriorhodopsin/amphipol complexes: structural and functional properties.
Biophys. J. 94:3523–3537.
Gohon, Y., Giusti, F., Prata, C., Charvolin, D., Timmins, P., Ebel, C., Tribet, C., Popot, J.-L. (2006) Well-defined
nanoparticles formed by hydrophobic assembly of a short and polydisperse random terpolymer, amphipol A8-35.
Langmuir 22:1281–1290.
Gorzelle, B.M., Hoffman, A.K., Keyes, M.H., Gray, D.N., Ray, D.G., Sanders II, C.R. (2002) Amphipols can support the
activity of a membrane enzyme. J. Am. Chem. Soc. 124:11594–11595.
Goyal, P., Krasteva, P.V., Van Gerven, N., Gubellini, F., Van den Broeck, I., Troupiotis-Tsaïlaki, A., Jonckheere, W.,
Péhau-Arnaudet, G., Pinkner, J.S., Chapman, M.R., Hultgren, S.J., Howorka, S., Fronzes, R., Remaut, H. (2014)
Structural and mechanistic insights into the bacterial amyloid secretion channel CsgG. Nature 516:250–253.
Gu, J., Wu, M., Guo, R., Yan, K., Lei, J., Gao, N., Yang, M. (2016) The architecture of the mammalian respirasome.
Nature 537:639–643.
Guénebaut, V., Schlitt, A., Weiss, H., Leonard, K., Friedrich, T. (1998) Consistent structure between bacterial and
mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Mol. Biol. 276:105–112.
Gulati, S., Jamshad, M., Knowles, T.J., Morrison, K.A., Downing, R., Cant, N., Collins, R., Koenderink, J.B., Ford, R.
C., Overduin, M., Kerr, I.D., Dafforn, T.R., Rothnie, A.J. (2014) Detergent-free purification of ABC (ATP-bindingcassette) transporters. Biochem. J. 461:269–278.
He, Y., Gao, X., Goswami, D., Hou, L., Pal, K., Yin, Y., Zhao, G., Ernst, O.P., Griffin, P., Melcher, K., Xu, H.E. (2017)
Molecular assembly of rhodopsin with G protein-coupled receptor kinases. Cell Res. 2017:1–20.
Henderson, R. (1995) The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of
unstained biological molecules. Quart. Rev. Biophys. 28:171–193.
Henderson, R. (2013) Ion channel seen by electron microscopy. Nature 504:93–94.
Henderson, R. (2015) Overview and future of single particle electron cryomicroscopy. Arch. Biochem. Biophys.
581:19–24.
Henderson, R., McMullan, G. (2013) Problems in obtaining perfect images by single-particle electron cryomicroscopy of
biological structures in amorphous ice. Microscopy (Oxf) 62:43–50.
Henderson, R., Sali, A., Baker, M.L., Carragher, B., Devkota, B., Downing, K.H., Egelman, E.H., Feng, Z., Frank, J.,
Grigorieff, N., Jiang, W., Ludtke, S.J., Medalia, O., Penczek, P.A., Rosenthal, P.B., Rossmann, M.G., Schmid, M.F.,
Schröder, G.F., Steven, A.C., Stokes, D.L., Westbrook, J.D., Wriggers, W., Yang, H., Young, J., Berman, H.M.,
Chiu, W., Kleywegt, G.J., Lawson, C.L. (2012) Outcome of the first electron microscopy validation task force
meeting. Structure 20:205–214.
Hoenger, A., Pagès, J.-M., Fourel, D., Engel, A. (1993) The orientation of porin OmpF in the outer membrane of
Escherichia coli. J. Mol. Biol. 233:400–413.
Huynh, K.W., Cohen, M.R., Chakrapani, S., Holdaway, H.A., Stewart, P.L., Moiseenkova-Bell, V.Y. (2014a) Structural
insight into the assembly of TRPV channels. Structure 22:260–268.
Huynh, K.W., Cohen, M.R., Jiang, J., Samanta, A., Lodowski, D.T., Zhou, H., Moiseenkova-Bell, V. (2016) Structure of
the full-length TRPV2 channel by cryo-EM. Nat. Commun. 7:1130.
Huynh, K.W., Cohen, M.R., Moiseenkova-Bell, V.Y. (2014b) Application of amphipols for structure-functional analysis
of TRP channels. J. Membr. Biol. 247:843–851.
Jeong, H., Kim, J.-S., Song, S., Shigematsu, H., Yokoyama, T., Hyun, J., Ha, N.-C. (2016) Pseudoatomic structure of the
tripartite multidrug efflux pump AcrAB-TolC reveals the intermeshing cogwheel-like interaction between AcrA and
TolC. Structure 24:272–276.
Jin, P., Bulkley, D., Guo, Y., Zhang, W., Guo, Z., Huynh, W., Wu, S., Meltzer, S., Cheng, T., Jan, L.Y., Jan, Y.-N.,
Cheng, Y. (2017) Electron cryo-microscopy structure of the mechanotransduction channel NOMPC. Nature
547:118–122.
Karlsson, G. (2001) Thickness measurements of lacey carbon films. J. Microsc. 203:326–328.
Kawate, T., Gouaux, E. (2006) Fluorescence-detection size-exclusion chromatography for precrystallization screening of
integral membrane proteins. Structure 14:673–681.
Kelly, D.F., Abeyrathne, P.D., Dukovski, D., Walz, T. (2008) The Affinity Grid: a pre-fabricated EM grid for monolayer
purification. J. Mol. Biol. 382:423–433.
586
12 The Use of Amphipols for Electron Microscopy
and stability of thin, cryo-EM specimens. Biophys. J. 110:749–755.
Goehring, A., Lee, C.-H., Wang, K.H., Michel, J.C., Claxton, D.P., Baconguis, I., Althoff, T., Fischer, S., Garcia, C.,
Gouaux, E. (2014) Screening and large-scale expression of membrane proteins in mammalian cells for structural
studies. Nat. Protoc. 9:2574–2585.
Gohon, Y. (2002) Etude structurale et fonctionnelle de deux protéines membranaires, la bactériorhodopsine et le
récepteur nicotinique de l'acétylcholine, maintenues en solution aqueuse non détergente par des polymères
amphiphiles. Université Paris-VI, Paris, 467 p.
Gohon, Y., Dahmane, T., Ruigrok, R., Schuck, P., Charvolin, D., Rappaport, F., Timmins, P., Engelman, D.M., Tribet,
C., Popot, J.-L., Ebel, C. (2008) Bacteriorhodopsin/amphipol complexes: structural and functional properties.
Biophys. J. 94:3523–3537.
Gohon, Y., Giusti, F., Prata, C., Charvolin, D., Timmins, P., Ebel, C., Tribet, C., Popot, J.-L. (2006) Well-defined
nanoparticles formed by hydrophobic assembly of a short and polydisperse random terpolymer, amphipol A8-35.
Langmuir 22:1281–1290.
Gorzelle, B.M., Hoffman, A.K., Keyes, M.H., Gray, D.N., Ray, D.G., Sanders II, C.R. (2002) Amphipols can support the
activity of a membrane enzyme. J. Am. Chem. Soc. 124:11594–11595.
Goyal, P., Krasteva, P.V., Van Gerven, N., Gubellini, F., Van den Broeck, I., Troupiotis-Tsaïlaki, A., Jonckheere, W.,
Péhau-Arnaudet, G., Pinkner, J.S., Chapman, M.R., Hultgren, S.J., Howorka, S., Fronzes, R., Remaut, H. (2014)
Structural and mechanistic insights into the bacterial amyloid secretion channel CsgG. Nature 516:250–253.
Gu, J., Wu, M., Guo, R., Yan, K., Lei, J., Gao, N., Yang, M. (2016) The architecture of the mammalian respirasome.
Nature 537:639–643.
Guénebaut, V., Schlitt, A., Weiss, H., Leonard, K., Friedrich, T. (1998) Consistent structure between bacterial and
mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Mol. Biol. 276:105–112.
Gulati, S., Jamshad, M., Knowles, T.J., Morrison, K.A., Downing, R., Cant, N., Collins, R., Koenderink, J.B., Ford, R.
C., Overduin, M., Kerr, I.D., Dafforn, T.R., Rothnie, A.J. (2014) Detergent-free purification of ABC (ATP-bindingcassette) transporters. Biochem. J. 461:269–278.
He, Y., Gao, X., Goswami, D., Hou, L., Pal, K., Yin, Y., Zhao, G., Ernst, O.P., Griffin, P., Melcher, K., Xu, H.E. (2017)
Molecular assembly of rhodopsin with G protein-coupled receptor kinases. Cell Res. 2017:1–20.
Henderson, R. (1995) The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of
unstained biological molecules. Quart. Rev. Biophys. 28:171–193.
Henderson, R. (2013) Ion channel seen by electron microscopy. Nature 504:93–94.
Henderson, R. (2015) Overview and future of single particle electron cryomicroscopy. Arch. Biochem. Biophys.
581:19–24.
Henderson, R., McMullan, G. (2013) Problems in obtaining perfect images by single-particle electron cryomicroscopy of
biological structures in amorphous ice. Microscopy (Oxf) 62:43–50.
Henderson, R., Sali, A., Baker, M.L., Carragher, B., Devkota, B., Downing, K.H., Egelman, E.H., Feng, Z., Frank, J.,
Grigorieff, N., Jiang, W., Ludtke, S.J., Medalia, O., Penczek, P.A., Rosenthal, P.B., Rossmann, M.G., Schmid, M.F.,
Schröder, G.F., Steven, A.C., Stokes, D.L., Westbrook, J.D., Wriggers, W., Yang, H., Young, J., Berman, H.M.,
Chiu, W., Kleywegt, G.J., Lawson, C.L. (2012) Outcome of the first electron microscopy validation task force
meeting. Structure 20:205–214.
Hoenger, A., Pagès, J.-M., Fourel, D., Engel, A. (1993) The orientation of porin OmpF in the outer membrane of
Escherichia coli. J. Mol. Biol. 233:400–413.
Huynh, K.W., Cohen, M.R., Chakrapani, S., Holdaway, H.A., Stewart, P.L., Moiseenkova-Bell, V.Y. (2014a) Structural
insight into the assembly of TRPV channels. Structure 22:260–268.
Huynh, K.W., Cohen, M.R., Jiang, J., Samanta, A., Lodowski, D.T., Zhou, H., Moiseenkova-Bell, V. (2016) Structure of
the full-length TRPV2 channel by cryo-EM. Nat. Commun. 7:1130.
Huynh, K.W., Cohen, M.R., Moiseenkova-Bell, V.Y. (2014b) Application of amphipols for structure-functional analysis
of TRP channels. J. Membr. Biol. 247:843–851.
Jeong, H., Kim, J.-S., Song, S., Shigematsu, H., Yokoyama, T., Hyun, J., Ha, N.-C. (2016) Pseudoatomic structure of the
tripartite multidrug efflux pump AcrAB-TolC reveals the intermeshing cogwheel-like interaction between AcrA and
TolC. Structure 24:272–276.
Jin, P., Bulkley, D., Guo, Y., Zhang, W., Guo, Z., Huynh, W., Wu, S., Meltzer, S., Cheng, T., Jan, L.Y., Jan, Y.-N.,
Cheng, Y. (2017) Electron cryo-microscopy structure of the mechanotransduction channel NOMPC. Nature
547:118–122.
Karlsson, G. (2001) Thickness measurements of lacey carbon films. J. Microsc. 203:326–328.
Kawate, T., Gouaux, E. (2006) Fluorescence-detection size-exclusion chromatography for precrystallization screening of
integral membrane proteins. Structure 14:673–681.
Kelly, D.F., Abeyrathne, P.D., Dukovski, D., Walz, T. (2008) The Affinity Grid: a pre-fabricated EM grid for monolayer
purification. J. Mol. Biol. 382:423–433.
586
12 The Use of Amphipols for Electron Microscopy