Wilkes, M., Madej, M.G., Kreuter, L., Rhinow, D., Heinz, V., De Sanctis, S., Ruppel, S., Richter, R.M., Joos, F.,
Grieben, M., Pike, A.C., Huiskonen, J.T., Carpenter, E.P., Kühlbrandt, W., Witzgall, R., Ziegler, C. (2017) Molecular
insights into lipid-assisted Ca
2+ regulation of the TRP channel polycystin-2. Nat. Struct. Mol. Biol. 24:123–130.
Wilkinson, M., Chaban, Y., Wigley, D.B. (2016a) Mechanism for nuclease regulation in RecBCD. eLIFE 5:e18227.
Wilkinson, M., Troman, L., Wan Nur Ismah, W.A.K., Chaban, Y., Avison, M.B., Dillingham, M.S., Wigley,
D.B. (2016b) Structural basis for the inhibition of RecBCD by Gam and its synergistic antibacterial effect with
quinolones. eLIFE 5:e22963.
Wisedchaisri, G., Reichow, S.L., Gonen, T. (2011) Advances in structural and functional analysis of membrane proteins
by electron crystallography. Structure 19:1381–1393.
Wojtowicz, H., Prochnicka-Chalufour, A., de Amorim, G.C., Roudenko, O., Simenel, C., Malki, I., Pehau-Arnaudet, G.,
Gubellini, F., Koutsioubas, A., Pérez, J., Delepelaire, P., Delepierre, M., Fronzes, R., Izadi-Pruneyre, N. (2016)
Structural basis of the signalling through a bacterial membrane receptor HasR deciphered by an integrative approach.
Biochem. J. 473:2239–2248.
Wong, W., Bai, X.-C., Brown, A., Fernandez, I.S., Hanssen, E., Condron, M., Tan, Y.H., Baum, J., Scheres,
S.H.W. (2014) Cryo-EM structure of the Plasmodium falciparum 80 S ribosome bound to the anti-protozoan drug
emetine. eLife 3:e03080.
Wu, Z.S., Cui, Z.C., Cheng, H., Fan, C., Melcher, K., Jiang, Y., Zhang, C.H., Jiang, H.L., Cong, Y., Liu, Q., Xu,
H.E. (2015) High yield and efficient expression and purification of the human 5-HT 3A receptor. Acta Pharmacol. Sin.
36:1024–1032.
Xu, J., Gui, M., Wang, D., Xiang, Y. (2016) The bacteriophage Φ29 tail possesses a pore-forming loop for cell
membrane penetration. Nature 534:544–547.
Yan, Z., Bai, X.-C., Yan, C., Wu, J., Li, Z., Wei, T.X., Peng, W., Yin, C.-C., Li, X., Scheres, S.H.W., Shi, Y., Yan,
N. (2015) Structure of the rabbit ryanodine receptor RyR1 at near-atomic resolution. Nature 517:50–55.
Yang, G., Zhou, R., Shi, Y. (2017) Cryo-EM structures of human γ-secretase. Curr. Opin. Struct. Biol. 46:55–64.
Zalk, R., Clarke, O.B., Georges, A., Grassucci, R.A., Reiken, S., Mancia, F., Hendrickson, W.A., Frank, J., Marks,
A.R. (2015) Structure of a mammalian ryanodine receptor. Nature 517:44–49.
Zhang, N., Tsybovsky, Y., Kolesnikov, A.V., Rozanowska, M., Swider, M., Schwartz, S.B., Stone, E.M., Palczewska,
G., Maeda, A., Kefalov, V.J., Jacobson, S.G., Cideciyan, A.V., Palczewski, K. (2015) Protein misfolding and the
pathogenesis of ABCA4-associated retinal degenerations. Hum. Mol. Genet. 24:3220–3237.
Zhou, X., Li, M., Su, D., Jia, Q., Li, H., Li, X., Yang, J. (2017) Cryo-EM structures of the human endolysosomal
TRPML3 channel in three distinct states. Nat. Struct. Mol. Biol. 24:1146–1154.
Zickermann, V., Kerscher, S., Zwicker, K., Tocilescua, M.A., Radermacher, M., Brand, U. (2009) Architecture of
complex I and its implications for electron transfer and proton pumping. Biochim. Biophys. Acta. 1787:574–583.
Zoonens, M., Catoire, L.J., Giusti, F., Popot, J.-L. (2005) NMR study of a membrane protein in detergent-free aqueous
solution. Proc. Natl. Acad. Sci. USA 102:8893–8898.
Zoonens, M., Giusti, F., Zito, F., Popot, J.-L. (2007) Dynamics of membrane protein/amphipol association studied by
Förster resonance energy transfer. Implications for in vitro studies of amphipol-stabilized membrane proteins.
Biochemistry 46:10392–10404.
Zorman, S., Botte, M., Jiang, Q., Collinson, I., Schaffitzel, C. (2015) Advances and challenges of membrane-protein
complex production. Curr. Opin. Struct. Biol. 32:123–130.
Zubcevic, L., Herzik, M.A., Jr., Chung, B.C., Liu, Z., Lander, G.C., Lee, S.-Y. (2016) Cryo-electron microscopy
structure of the TRPV2 ion channel. Nat. Struct. Mol. Biol. 23:180–186.
590
12 The Use of Amphipols for Electron Microscopy
Grieben, M., Pike, A.C., Huiskonen, J.T., Carpenter, E.P., Kühlbrandt, W., Witzgall, R., Ziegler, C. (2017) Molecular
insights into lipid-assisted Ca
2+ regulation of the TRP channel polycystin-2. Nat. Struct. Mol. Biol. 24:123–130.
Wilkinson, M., Chaban, Y., Wigley, D.B. (2016a) Mechanism for nuclease regulation in RecBCD. eLIFE 5:e18227.
Wilkinson, M., Troman, L., Wan Nur Ismah, W.A.K., Chaban, Y., Avison, M.B., Dillingham, M.S., Wigley,
D.B. (2016b) Structural basis for the inhibition of RecBCD by Gam and its synergistic antibacterial effect with
quinolones. eLIFE 5:e22963.
Wisedchaisri, G., Reichow, S.L., Gonen, T. (2011) Advances in structural and functional analysis of membrane proteins
by electron crystallography. Structure 19:1381–1393.
Wojtowicz, H., Prochnicka-Chalufour, A., de Amorim, G.C., Roudenko, O., Simenel, C., Malki, I., Pehau-Arnaudet, G.,
Gubellini, F., Koutsioubas, A., Pérez, J., Delepelaire, P., Delepierre, M., Fronzes, R., Izadi-Pruneyre, N. (2016)
Structural basis of the signalling through a bacterial membrane receptor HasR deciphered by an integrative approach.
Biochem. J. 473:2239–2248.
Wong, W., Bai, X.-C., Brown, A., Fernandez, I.S., Hanssen, E., Condron, M., Tan, Y.H., Baum, J., Scheres,
S.H.W. (2014) Cryo-EM structure of the Plasmodium falciparum 80 S ribosome bound to the anti-protozoan drug
emetine. eLife 3:e03080.
Wu, Z.S., Cui, Z.C., Cheng, H., Fan, C., Melcher, K., Jiang, Y., Zhang, C.H., Jiang, H.L., Cong, Y., Liu, Q., Xu,
H.E. (2015) High yield and efficient expression and purification of the human 5-HT 3A receptor. Acta Pharmacol. Sin.
36:1024–1032.
Xu, J., Gui, M., Wang, D., Xiang, Y. (2016) The bacteriophage Φ29 tail possesses a pore-forming loop for cell
membrane penetration. Nature 534:544–547.
Yan, Z., Bai, X.-C., Yan, C., Wu, J., Li, Z., Wei, T.X., Peng, W., Yin, C.-C., Li, X., Scheres, S.H.W., Shi, Y., Yan,
N. (2015) Structure of the rabbit ryanodine receptor RyR1 at near-atomic resolution. Nature 517:50–55.
Yang, G., Zhou, R., Shi, Y. (2017) Cryo-EM structures of human γ-secretase. Curr. Opin. Struct. Biol. 46:55–64.
Zalk, R., Clarke, O.B., Georges, A., Grassucci, R.A., Reiken, S., Mancia, F., Hendrickson, W.A., Frank, J., Marks,
A.R. (2015) Structure of a mammalian ryanodine receptor. Nature 517:44–49.
Zhang, N., Tsybovsky, Y., Kolesnikov, A.V., Rozanowska, M., Swider, M., Schwartz, S.B., Stone, E.M., Palczewska,
G., Maeda, A., Kefalov, V.J., Jacobson, S.G., Cideciyan, A.V., Palczewski, K. (2015) Protein misfolding and the
pathogenesis of ABCA4-associated retinal degenerations. Hum. Mol. Genet. 24:3220–3237.
Zhou, X., Li, M., Su, D., Jia, Q., Li, H., Li, X., Yang, J. (2017) Cryo-EM structures of the human endolysosomal
TRPML3 channel in three distinct states. Nat. Struct. Mol. Biol. 24:1146–1154.
Zickermann, V., Kerscher, S., Zwicker, K., Tocilescua, M.A., Radermacher, M., Brand, U. (2009) Architecture of
complex I and its implications for electron transfer and proton pumping. Biochim. Biophys. Acta. 1787:574–583.
Zoonens, M., Catoire, L.J., Giusti, F., Popot, J.-L. (2005) NMR study of a membrane protein in detergent-free aqueous
solution. Proc. Natl. Acad. Sci. USA 102:8893–8898.
Zoonens, M., Giusti, F., Zito, F., Popot, J.-L. (2007) Dynamics of membrane protein/amphipol association studied by
Förster resonance energy transfer. Implications for in vitro studies of amphipol-stabilized membrane proteins.
Biochemistry 46:10392–10404.
Zorman, S., Botte, M., Jiang, Q., Collinson, I., Schaffitzel, C. (2015) Advances and challenges of membrane-protein
complex production. Curr. Opin. Struct. Biol. 32:123–130.
Zubcevic, L., Herzik, M.A., Jr., Chung, B.C., Liu, Z., Lander, G.C., Lee, S.-Y. (2016) Cryo-electron microscopy
structure of the TRPV2 ion channel. Nat. Struct. Mol. Biol. 23:180–186.
590
12 The Use of Amphipols for Electron Microscopy