Althoff, T. (2011) Strukturelle Untersuchungen am Superkomplex I 1 III 2 IV 1 der Atmungskette mittels Kryoelektronenmikroskopie, Fachbereich Biochemie, Chemie und Pharmazie. Johann Wolfgang Goethe-Universität, Frankfurt-amMain, 248 p.
Althoff, T., Mills, D.J., Popot, J.-L., Kühlbrandt, W. (2011) Assembly of electron transport chain components in bovine
mitochondrial supercomplex I 1 III 2 IV 1 . EMBO J. 30:4652–4664.
Amunts, A., Brown, A., Bai, X.-C., Llácer, J.L., Hussain, T., Emsley, P., Long, F., Murshudov, G., Scheres, S.H.W.,
Ramakrishnan, V. (2014) Structure of the yeast mitochondrial large ribosomal subunit. Science 343:1485–1489.
Arnaud, C.-A., Effantin, G., Vivès, C., Engilberge, S., Bacia, M., Boulanger, P., Girard, E., Schoehn, G., Breyton, C.
(2017) Bacteriophage T5 tail tube structure suggests a trigger mechanism for Siphoviridae DNA ejection. Nat. Comm.
8:1953.
Arunmanee, W., Harris, J.R., Lakey, J.H. (2014) Outer membrane protein F stabilised with minimal amphipol forms
linear arrays and LPS-dependent 2D crystals. J. Membr. Biol. 247:949–956.
Baboolal, T.G., Conroy, M.J., Gill, K., Ridley, H., Visudtiphole, V., Bullough, P.A., Lakey, J.H. (2008) Colicin N binds
to the periphery of its receptor and translocator, outer membrane protein F. Structure 16:371–379.
Bai, X.-C., McMullan, G., Scheres, S.H.W. (2015a) How cryo-EM is revolutionizing structural biology. Trends
Biochem. Sci. 40:49–57.
Bai, X.-C., Rajendra, E., Yang, G., Shi, Y., Scheres, S.H.W. (2015b) Sampling the conformational space of the catalytic
subunit of human γ-secretase. eLIFE 4:e11182.
Bai, X.-C., Yan, C., Yang, G., Lu, P., Ma, D., Sun, L., Zhou, R., Scheres, S.H.W., Shi, Y. (2015c) An atomic structure of
human γ-secretase. Nature 525:212–218.
Baker, M.R., Fan, G., Serysheva, I.I. (2015) Single-particle cryo-EM of the ryanodine receptor channel in an aqueous
environment. Eur. J. Transl. Myol. 25:35–48.
Bausewein, T., Mills, D.J., Langer, J.D., Nitschke, B., Nussberger, S., Kühlbrandt, W. (2017) Cryo-EM structure of the
TOM core complex from Neurospora crassa. Cell 170:693–700.e697.
Bazzacco, P., Billon-Denis, E., Sharma, K.S., Catoire, L.J., Mary, S., Le Bon, C., Point, E., Banères, J.-L., Durand, G.,
Zito, F., Pucci, B., Popot, J.-L. (2012) Non-ionic homopolymeric amphipols: Application to membrane protein
folding, cell-free synthesis, and solution NMR. Biochemistry 51:1416–1430.
Beckham, K.S., Ciccarelli, L., Bunduc, C.M., Mertens, H.D., Ummels, R., Lugmayr, W., Mayr, J., Rettel, M., Savitski,
M.M., Svergun, D.I., Bitter, W., Wilmanns, M., Marlovits, T.C., Parret, A.H., Houben, E.N. (2017) Structure of the
mycobacterial ESX-5 type VII secretion system membrane complex by single-particle analysis. Nat. Microbiol.
2:17047.
Botte, M., Zaccai, N.R., Lycklama à Nijeholt, J., Martin, R., Knoops, K., Papai, G., Zou, J., Deniaud, A., Karuppasamy,
M., Jiang, Q., Singha Roy, A., Schulten, K., Schultz, P., Rappsilber, J., Zaccai, G., Berger, I., Collinson, I.,
Schaffitzel, C. (2016) A central cavity within the holotranslocon suggests a mechanism for membrane protein
insertion. Sci. Rep. 6:38399.
Breyton, C., Tribet, C., Olive, J., Dubacq, J.-P., Popot, J.-L. (1997) Dimer to monomer conversion of the cytochrome
b 6 f complex: causes and consequences. J. Biol. Chem. 272:21892–21900.
Callaway, E. (2015) The revolution will not be crystallized. Nature 525:172–174.
Cao, E., Cordero-Morales, J.F., Liu, B., Qin, F., Julius, D. (2013a) TRPV1 channels are intrinsically heat sensitive and
negatively regulated by phosphoinositide lipids. Neuron 77:667–679.
Cao, E., Liao, M., Cheng, Y., Julius, D. (2013b) TRPV1 structures in distinct conformations reveal activation
mechanisms. Nature 504:113–118.
Carazo, J.M., Sorzano, C.O.S., Otón, J., Marabini, R., Vargas, J. (2015) Three-dimensional reconstruction methods in
single-particle analysis from transmission electron microscopy data. Arch. Biochem. Biophys. 581:39–48.
Catoire, L.J., Zoonens, M., van Heijenoort, C., Giusti, F., Popot, J.-L., Guittet, E. (2009) Inter- and intramolecular
contacts in a membrane protein/surfactant complex observed by heteronuclear dipole-to-dipole cross-relaxation.
J. Magn. Res. 197:91–95.
Catoire, L.J., Zoonens, M., van Heijenoort, C., Giusti, F., Guittet, E., Popot, J.-L. (2010) Solution NMR mapping of
water-accessible residues in the transmembrane β-barrel of OmpX. Eur. Biophys. J. 39:623–630.
Champeil, P., Menguy, T., Tribet, C., Popot, J.-L., le Maire, M. (2000) Interaction of amphipols with the sarcoplasmic
reticulum Ca
2+ -ATPase. J. Biol. Chem. 275:18623–18637.
Charvolin, D., Perez, J.-B., Rouvière, F., Giusti, F., Bazzacco, P., Abdine, A., Rappaport, F., Martinez, K.L., Popot, J.-L.
(2009) The use of amphipols as universal molecular adapters to immobilize membrane proteins onto solid supports.
Proc. Natl. Acad. Sci. USA 106:405–410.
Chen, Y., Clarke, O.B., Kim, J., Stowe, S., Kim, Y.-K., Assur, Z., Cavalier, C., Godoy-Ruiz, R., von Alpen, D.C.,
Manzini, C., Blaner, W.S., Frank, J., Quadro, L., Weber, D.J., Shapiro, L., Hendrickson, W.A., Mancia, F. (2016)
Structure of the STRA6 receptor for retinol uptake. Science 353:pii aad 8266–8261.
Cheng, Y. (2015) Single-particle cryo-EM at crystallographic resolution. Cell 161:450–457.
584
12 The Use of Amphipols for Electron Microscopy
Althoff, T., Mills, D.J., Popot, J.-L., Kühlbrandt, W. (2011) Assembly of electron transport chain components in bovine
mitochondrial supercomplex I 1 III 2 IV 1 . EMBO J. 30:4652–4664.
Amunts, A., Brown, A., Bai, X.-C., Llácer, J.L., Hussain, T., Emsley, P., Long, F., Murshudov, G., Scheres, S.H.W.,
Ramakrishnan, V. (2014) Structure of the yeast mitochondrial large ribosomal subunit. Science 343:1485–1489.
Arnaud, C.-A., Effantin, G., Vivès, C., Engilberge, S., Bacia, M., Boulanger, P., Girard, E., Schoehn, G., Breyton, C.
(2017) Bacteriophage T5 tail tube structure suggests a trigger mechanism for Siphoviridae DNA ejection. Nat. Comm.
8:1953.
Arunmanee, W., Harris, J.R., Lakey, J.H. (2014) Outer membrane protein F stabilised with minimal amphipol forms
linear arrays and LPS-dependent 2D crystals. J. Membr. Biol. 247:949–956.
Baboolal, T.G., Conroy, M.J., Gill, K., Ridley, H., Visudtiphole, V., Bullough, P.A., Lakey, J.H. (2008) Colicin N binds
to the periphery of its receptor and translocator, outer membrane protein F. Structure 16:371–379.
Bai, X.-C., McMullan, G., Scheres, S.H.W. (2015a) How cryo-EM is revolutionizing structural biology. Trends
Biochem. Sci. 40:49–57.
Bai, X.-C., Rajendra, E., Yang, G., Shi, Y., Scheres, S.H.W. (2015b) Sampling the conformational space of the catalytic
subunit of human γ-secretase. eLIFE 4:e11182.
Bai, X.-C., Yan, C., Yang, G., Lu, P., Ma, D., Sun, L., Zhou, R., Scheres, S.H.W., Shi, Y. (2015c) An atomic structure of
human γ-secretase. Nature 525:212–218.
Baker, M.R., Fan, G., Serysheva, I.I. (2015) Single-particle cryo-EM of the ryanodine receptor channel in an aqueous
environment. Eur. J. Transl. Myol. 25:35–48.
Bausewein, T., Mills, D.J., Langer, J.D., Nitschke, B., Nussberger, S., Kühlbrandt, W. (2017) Cryo-EM structure of the
TOM core complex from Neurospora crassa. Cell 170:693–700.e697.
Bazzacco, P., Billon-Denis, E., Sharma, K.S., Catoire, L.J., Mary, S., Le Bon, C., Point, E., Banères, J.-L., Durand, G.,
Zito, F., Pucci, B., Popot, J.-L. (2012) Non-ionic homopolymeric amphipols: Application to membrane protein
folding, cell-free synthesis, and solution NMR. Biochemistry 51:1416–1430.
Beckham, K.S., Ciccarelli, L., Bunduc, C.M., Mertens, H.D., Ummels, R., Lugmayr, W., Mayr, J., Rettel, M., Savitski,
M.M., Svergun, D.I., Bitter, W., Wilmanns, M., Marlovits, T.C., Parret, A.H., Houben, E.N. (2017) Structure of the
mycobacterial ESX-5 type VII secretion system membrane complex by single-particle analysis. Nat. Microbiol.
2:17047.
Botte, M., Zaccai, N.R., Lycklama à Nijeholt, J., Martin, R., Knoops, K., Papai, G., Zou, J., Deniaud, A., Karuppasamy,
M., Jiang, Q., Singha Roy, A., Schulten, K., Schultz, P., Rappsilber, J., Zaccai, G., Berger, I., Collinson, I.,
Schaffitzel, C. (2016) A central cavity within the holotranslocon suggests a mechanism for membrane protein
insertion. Sci. Rep. 6:38399.
Breyton, C., Tribet, C., Olive, J., Dubacq, J.-P., Popot, J.-L. (1997) Dimer to monomer conversion of the cytochrome
b 6 f complex: causes and consequences. J. Biol. Chem. 272:21892–21900.
Callaway, E. (2015) The revolution will not be crystallized. Nature 525:172–174.
Cao, E., Cordero-Morales, J.F., Liu, B., Qin, F., Julius, D. (2013a) TRPV1 channels are intrinsically heat sensitive and
negatively regulated by phosphoinositide lipids. Neuron 77:667–679.
Cao, E., Liao, M., Cheng, Y., Julius, D. (2013b) TRPV1 structures in distinct conformations reveal activation
mechanisms. Nature 504:113–118.
Carazo, J.M., Sorzano, C.O.S., Otón, J., Marabini, R., Vargas, J. (2015) Three-dimensional reconstruction methods in
single-particle analysis from transmission electron microscopy data. Arch. Biochem. Biophys. 581:39–48.
Catoire, L.J., Zoonens, M., van Heijenoort, C., Giusti, F., Popot, J.-L., Guittet, E. (2009) Inter- and intramolecular
contacts in a membrane protein/surfactant complex observed by heteronuclear dipole-to-dipole cross-relaxation.
J. Magn. Res. 197:91–95.
Catoire, L.J., Zoonens, M., van Heijenoort, C., Giusti, F., Guittet, E., Popot, J.-L. (2010) Solution NMR mapping of
water-accessible residues in the transmembrane β-barrel of OmpX. Eur. Biophys. J. 39:623–630.
Champeil, P., Menguy, T., Tribet, C., Popot, J.-L., le Maire, M. (2000) Interaction of amphipols with the sarcoplasmic
reticulum Ca
2+ -ATPase. J. Biol. Chem. 275:18623–18637.
Charvolin, D., Perez, J.-B., Rouvière, F., Giusti, F., Bazzacco, P., Abdine, A., Rappaport, F., Martinez, K.L., Popot, J.-L.
(2009) The use of amphipols as universal molecular adapters to immobilize membrane proteins onto solid supports.
Proc. Natl. Acad. Sci. USA 106:405–410.
Chen, Y., Clarke, O.B., Kim, J., Stowe, S., Kim, Y.-K., Assur, Z., Cavalier, C., Godoy-Ruiz, R., von Alpen, D.C.,
Manzini, C., Blaner, W.S., Frank, J., Quadro, L., Weber, D.J., Shapiro, L., Hendrickson, W.A., Mancia, F. (2016)
Structure of the STRA6 receptor for retinol uptake. Science 353:pii aad 8266–8261.
Cheng, Y. (2015) Single-particle cryo-EM at crystallographic resolution. Cell 161:450–457.
584
12 The Use of Amphipols for Electron Microscopy