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288:36272–36284.
Khoshouei, M., Radjainia, M., Baumeister, W., Danev, R. (2017) Cryo-EM structure of haemoglobin at 3.2 Å
determined with the Volta phase plate. Nat. Commun. 8:16099.
Klammt, C., Perrin, M.-H., Maslennikov, I., Renault, L., Krupa, M., Kwiatkowski, W., Stahlberg, H., Vale, W., Choe,
S. (2011) Polymer-based cell-free expression of ligand-binding family B G-protein coupled receptors without
detergents. Prot. Sci. 20:1030–1041.
Kühlbrandt, W. (2013) Introduction to electron crystallography. Methods Mol. Biol. 955:1–16.
Kühlbrandt, W. (2014a) Cryo-EM enters a new era. eLife:e03678.
Kühlbrandt, W. (2014b) The resolution revolution. Science 343:1443–1444.
Kühlbrandt, W. (2015) Structure and function of mitochondrial membrane protein complexes. BMC Biol. 13:89.
Lau, W.C., Rubinstein, J.L. (2013) Single-particle electron microscopy. Methods Mol. Biol. 955:401–426.
Le Bon, C., Della Pia, E.A., Giusti, F., Lloret, N., Zoonens, M., Martinez, K.L., Popot, J.-L. (2014a) Synthesis of an
oligonucleotide-derivatized amphipol and its use to trap and immobilize membrane proteins. Nucleic Acids Res.
42:e83.
Le Bon, C., Popot, J.-L., Giusti, F. (2014b) Labeling and functionalizing amphipols for biological applications.
J. Membr. Biol. 247:797–814.
Leis, A., Rockel, B., Andrees, L., Baumeister, W. (2009) Visualizing cells at the nanoscale. Trends Biochem. Sci.
34:60–70.
Letts, J.A., Fiedorczuk, K., Sazanov, L.A. (2016) The architecture of respiratory supercomplexes. Nature 537:644–648.
Lewis, B.A., Engelman, D.M. (1983) Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles. J. Mol. Biol. 166:211–217.
Li, M., Zhang, W.K., Benvin, N.M., Zhou, X., Su, D., Li, H., Wang, S., Michailidis, I.E., Tong, L., Li, X.,
Yang, J. (2017a) Structural basis of dual Ca
2+ /pH regulation of the endolysosomal TRPML1 channel. Nat. Struct.
Mol. Biol. 24:205–213.
Li, M., Zhou, X., Wang, S., Michailidis, I., Gong, Y., Su, D., Li, H., Li, X., Yang, J. (2017b) Structure of a eukaryotic
cyclic-nucleotide-gated channel. Nature 542:60–65.
Li, X., Mooney, P., Zheng, S., Booth, C.R., Braunfeld, M.B., Gubbens, S., Agard, D.A., Cheng, Y. (2013) Electron
counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat. Meth.
10:584–590.
Liao, M., Cao, E., Julius, D., Cheng, Y. (2013) Structure of the TRPV1 ion channel determined by electron cryomicroscopy. Nature 504:107–112.
Liao, M., Cao, E., Julius, D., Cheng, Y. (2014) Single-particle electron cryo-microscopy of a mammalian ion channel.
Curr. Opin. Struct. Biol. 27:1–7.
Lu, P., Bai, X.-C., Ma, D., Xie, T., Yan, C., Sun, L., Yang, G., Zhao, Y., Zhou, R., Scheres, S.H.W., Shi, Y. (2014)
Three-dimensional structure of human γ-secretase. Nature 512:166–170.
Lučič, V., Rigort, A., Baumeister, W. (2013) Cryo-electron tomography: the challenge of doing structural biology in situ.
J. Cell Biol. 202:407–419.
Madej, M.G., Ziegler, C.M. (2018) Dawning of a new era in TRP channel structural biology by cryo-electron
microscopy. Pflügers Archiv - Eur. J. Physiol. 470:213–225.
Martinez, K.L., Gohon, Y., Corringer, P.-J., Tribet, C., Mérola, F., Changeux, J.-P., Popot, J.-L. (2002) Allosteric
transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: molecular interactions vs. physical
constraints. FEBS Lett. 528:251–256.
Mazhab-Jafari, M.T., Rubinstein, J.L. (2016) Cryo-EM studies of the structure and dynamics of vacuolar-type ATPases.
Sci. Adv. 2:e1600725.
Milne, J.L., Borgnia, M.J., Bartesaghi, A., Tran, E.E., Earl, L.A., Schauder, D.M., Lengyel, J., Pierson, J., Patwardhan,
A., Subramaniam, S. (2013) Cryo-electron microscopy—a primer for the non-microscopist. FEBS J. 280:28–45.
Miyaguchi, K. (2014) Direct imaging electron microscopy (EM) methods in modern structural biology: Overview and
comparison with X-ray crystallography and single-particle cryo-EM reconstruction in the studies of large
macromolecules. Biol. Cell 106:323–345.
Murakami, S., Nakashima, R., Yamashita, E., Yamaguchi, A. (2002) Crystal structure of bacterial multidrug efflux
transporter AcrB. Nature 419:587–593.
Nagy, J.K., Kuhn Hoffmann, A., Keyes, M.H., Gray, D.N., Oxenoid, K., Sanders, C.R. (2001) Use of amphipathic
polymers to deliver a membrane protein to lipid bilayers. FEBS Lett. 501:115–120.
Nogales, E., Scheres, S.H.W. (2015) Cryo-EM: A unique tool for the visualization of macromolecular complexity. Mol.
Cell 58:677–689.
Ohi, M., Li, Y., Cheng, Y., Walz, T. (2004) Negative staining and image classification – powerful tools in modern
electron microscopy. Biol. Proced. Online 6:23–34.
References
587
functional analysis of the native peripherin-ROM1 complex isolated from photoreceptor cells. J. Biol. Chem.
288:36272–36284.
Khoshouei, M., Radjainia, M., Baumeister, W., Danev, R. (2017) Cryo-EM structure of haemoglobin at 3.2 Å
determined with the Volta phase plate. Nat. Commun. 8:16099.
Klammt, C., Perrin, M.-H., Maslennikov, I., Renault, L., Krupa, M., Kwiatkowski, W., Stahlberg, H., Vale, W., Choe,
S. (2011) Polymer-based cell-free expression of ligand-binding family B G-protein coupled receptors without
detergents. Prot. Sci. 20:1030–1041.
Kühlbrandt, W. (2013) Introduction to electron crystallography. Methods Mol. Biol. 955:1–16.
Kühlbrandt, W. (2014a) Cryo-EM enters a new era. eLife:e03678.
Kühlbrandt, W. (2014b) The resolution revolution. Science 343:1443–1444.
Kühlbrandt, W. (2015) Structure and function of mitochondrial membrane protein complexes. BMC Biol. 13:89.
Lau, W.C., Rubinstein, J.L. (2013) Single-particle electron microscopy. Methods Mol. Biol. 955:401–426.
Le Bon, C., Della Pia, E.A., Giusti, F., Lloret, N., Zoonens, M., Martinez, K.L., Popot, J.-L. (2014a) Synthesis of an
oligonucleotide-derivatized amphipol and its use to trap and immobilize membrane proteins. Nucleic Acids Res.
42:e83.
Le Bon, C., Popot, J.-L., Giusti, F. (2014b) Labeling and functionalizing amphipols for biological applications.
J. Membr. Biol. 247:797–814.
Leis, A., Rockel, B., Andrees, L., Baumeister, W. (2009) Visualizing cells at the nanoscale. Trends Biochem. Sci.
34:60–70.
Letts, J.A., Fiedorczuk, K., Sazanov, L.A. (2016) The architecture of respiratory supercomplexes. Nature 537:644–648.
Lewis, B.A., Engelman, D.M. (1983) Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles. J. Mol. Biol. 166:211–217.
Li, M., Zhang, W.K., Benvin, N.M., Zhou, X., Su, D., Li, H., Wang, S., Michailidis, I.E., Tong, L., Li, X.,
Yang, J. (2017a) Structural basis of dual Ca
2+ /pH regulation of the endolysosomal TRPML1 channel. Nat. Struct.
Mol. Biol. 24:205–213.
Li, M., Zhou, X., Wang, S., Michailidis, I., Gong, Y., Su, D., Li, H., Li, X., Yang, J. (2017b) Structure of a eukaryotic
cyclic-nucleotide-gated channel. Nature 542:60–65.
Li, X., Mooney, P., Zheng, S., Booth, C.R., Braunfeld, M.B., Gubbens, S., Agard, D.A., Cheng, Y. (2013) Electron
counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat. Meth.
10:584–590.
Liao, M., Cao, E., Julius, D., Cheng, Y. (2013) Structure of the TRPV1 ion channel determined by electron cryomicroscopy. Nature 504:107–112.
Liao, M., Cao, E., Julius, D., Cheng, Y. (2014) Single-particle electron cryo-microscopy of a mammalian ion channel.
Curr. Opin. Struct. Biol. 27:1–7.
Lu, P., Bai, X.-C., Ma, D., Xie, T., Yan, C., Sun, L., Yang, G., Zhao, Y., Zhou, R., Scheres, S.H.W., Shi, Y. (2014)
Three-dimensional structure of human γ-secretase. Nature 512:166–170.
Lučič, V., Rigort, A., Baumeister, W. (2013) Cryo-electron tomography: the challenge of doing structural biology in situ.
J. Cell Biol. 202:407–419.
Madej, M.G., Ziegler, C.M. (2018) Dawning of a new era in TRP channel structural biology by cryo-electron
microscopy. Pflügers Archiv - Eur. J. Physiol. 470:213–225.
Martinez, K.L., Gohon, Y., Corringer, P.-J., Tribet, C., Mérola, F., Changeux, J.-P., Popot, J.-L. (2002) Allosteric
transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: molecular interactions vs. physical
constraints. FEBS Lett. 528:251–256.
Mazhab-Jafari, M.T., Rubinstein, J.L. (2016) Cryo-EM studies of the structure and dynamics of vacuolar-type ATPases.
Sci. Adv. 2:e1600725.
Milne, J.L., Borgnia, M.J., Bartesaghi, A., Tran, E.E., Earl, L.A., Schauder, D.M., Lengyel, J., Pierson, J., Patwardhan,
A., Subramaniam, S. (2013) Cryo-electron microscopy—a primer for the non-microscopist. FEBS J. 280:28–45.
Miyaguchi, K. (2014) Direct imaging electron microscopy (EM) methods in modern structural biology: Overview and
comparison with X-ray crystallography and single-particle cryo-EM reconstruction in the studies of large
macromolecules. Biol. Cell 106:323–345.
Murakami, S., Nakashima, R., Yamashita, E., Yamaguchi, A. (2002) Crystal structure of bacterial multidrug efflux
transporter AcrB. Nature 419:587–593.
Nagy, J.K., Kuhn Hoffmann, A., Keyes, M.H., Gray, D.N., Oxenoid, K., Sanders, C.R. (2001) Use of amphipathic
polymers to deliver a membrane protein to lipid bilayers. FEBS Lett. 501:115–120.
Nogales, E., Scheres, S.H.W. (2015) Cryo-EM: A unique tool for the visualization of macromolecular complexity. Mol.
Cell 58:677–689.
Ohi, M., Li, Y., Cheng, Y., Walz, T. (2004) Negative staining and image classification – powerful tools in modern
electron microscopy. Biol. Proced. Online 6:23–34.
References
587