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16:16.
Stahlberg, H., Biyani, N., Engel, A. (2015) 3D reconstruction of two-dimensional crystals. Arch. Biochem. Biophys.
581:68–77.
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286:1700–1705.
Suárez-Suárez, S., Carriedo, G.A., Presa Soto, A. (2013) Gold-decorated chiral macroporous films by the self-assembly
of functionalised block copolymers. Chem. Eur. J. 19:15933–15940.
Sun, L., Zhao, L., Yang, G., Yan, C., Zhou, R., Zhou, X., Xie, T., Zhao, Y., Wu, S., Li, X., Shi, Y. (2015) Structural basis
of human γ-secretase assembly. Proc. Natl. Acad. Sci. USA 112:6003–6008.
Sverzhinsky, A., Qian, S., Yang, L., Allaire, M., Moraes, I., Ma, D., Chung, J.W., Zoonens, M., Popot, J.-L., Coulton,
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Tribet, C., Diab, C., Dahmane, T., Zoonens, M., Popot, J.-L., Winnik, F.M. (2009) Thermodynamic characterization of
the exchange of detergents and amphipols at the surfaces of integral membrane proteins. Langmuir 25:12623–12634.
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conformational changes of ABCA4, the photoreceptor-specific ABC transporter. Structure 21:854–860.
Ubarretxena-Belandia, I., Stokes, D.L. (2010) Present and future of membrane protein structure determination by
electron crystallography. Adv. Protein Chem. Struct. Biol. 81:33–60.
Vahedi-Faridi, A., Jastrzebska, B., Palczewski, K., Engel, A. (2013) 3D imaging and quantitative analysis of small
solubilized membrane proteins and their complexes by transmission electron microscopy. Microscopy (Oxf)
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van Pee, K., Neuhaus, A., D’Imprima, E., Mills, D.J., Kühlbrandt, W., Yildiz, Ö. (2017) CryoEM structures of membrane
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Venkatachalam, K., Montell, C. (2007) TRP channels. Annu. Rev. Biochem. 76:387–417.
Villa, E., Schaffer, M., Plitzko, J.M., Baumeister, W. (2013) Opening windows into the cell: focused-ion-beam milling
for cryo-electron tomography. Curr. Opin. Struct. Biol. 23:771–777.
Vinothkumar, K.R., Zhu, J., Hirst, J. (2014) Architecture of mammalian respiratory complex I. Nature 515:80–84.
Vinothkumar, K.R. (2015) Membrane protein structures without crystals, by single-particle electron cryomicroscopy.
Curr. Opin. Struct. Biol. 33:103–114.
Vinothkumar, K.R., Henderson, R. (2016) Single-particle electron cryomicroscopy: trends, issues and future perspective.
Q. Rev. Biophys. 49:e13.
Wang, Z., Fan, G., Hryc, C.F., Blaza, J.N., Serysheva, I.I., Schmid, M.F., Chiu, W., Luisi, B.F., Du, D. (2017) An
allosteric transport mechanism for the AcrAB-TolC multidrug efflux pump. eLife 6:e24905.
Wei, R., Wang, X., Zhang, Y., Mukherjee, S., Zhang, L., Chen, Q., Huang, X., Jing, S., Liu, C., Li, S., Wang, G., Xu, Y.,
Zhu, S., Williams, A.J., Sun, F., C.C. Y. (2016) Structural insights into Ca
2+ -activated long-range allosteric channel
gating of RyR1. Cell Res. 26:977–994.
Wilkens, S. (2000) F 1 F O -ATP synthase–stalking mind and imagination. J. Bioenerg. Biomembr. 32:333–339.
Wilkens, S., Capaldi, R.A. (1998a) Electron microscopic evidence of two stalks linking the F 1 and F O parts of the
Escherichia coli ATP synthase. Biochim. Biophys. Acta 1365:93–97.
Wilkens, S., Capaldi, R.A. (1998b) ATP synthase’s second stalk comes into focus. Nature 393:29.
Wilkens, S., Zhou, J., Nakayama, R., Dunn, S.D., Capaldi, R.A. (2000) Localization of the δ subunit in the Escherichia
coli F 1 F O -ATPsynthase by immuno-electron microscopy: The δ subunit binds on top of the F 1 . J. Mol. Biol.
295:387–391.
References
589
respirasome. eLIFE 5:e21290.
Spear, J.M., Koborssy, D.A., Schwartz, A.B., Johnson, A.J., Audhya, A., Fadool, D.A., Stagg, S.M. (2015) Kv1.3
contains an alternative C-terminal ER exit motif and is recruited into COPII vesicles by Sec24a. BMC Biochem.
16:16.
Stahlberg, H., Biyani, N., Engel, A. (2015) 3D reconstruction of two-dimensional crystals. Arch. Biochem. Biophys.
581:68–77.
Stark, H., Chari, A. (2016) Sample preparation of biological macromolecular assemblies for the determination of highresolution structures by cryo-electron microscopy. Microscopy (Oxf) 65:23–34.
Stock, D., Leslie, A.G.W., Walker, J.E. (1999) Molecular architecture of the rotary motor in ATP synthase. Science
286:1700–1705.
Suárez-Suárez, S., Carriedo, G.A., Presa Soto, A. (2013) Gold-decorated chiral macroporous films by the self-assembly
of functionalised block copolymers. Chem. Eur. J. 19:15933–15940.
Sun, L., Zhao, L., Yang, G., Yan, C., Zhou, R., Zhou, X., Xie, T., Zhao, Y., Wu, S., Li, X., Shi, Y. (2015) Structural basis
of human γ-secretase assembly. Proc. Natl. Acad. Sci. USA 112:6003–6008.
Sverzhinsky, A., Qian, S., Yang, L., Allaire, M., Moraes, I., Ma, D., Chung, J.W., Zoonens, M., Popot, J.-L., Coulton,
J.W. (2014) Amphipol-trapped ExbB-ExbD membrane protein complex from Escherichia coli: A biochemical and
structural case study. J. Membr. Biol. 247:1005–1018.
Terahara, T., Kodera, N., Uchihashi, T., Ando, T., Namba, K., Minamino, T. (2017) Na
+ -induced structural transition of
MotPS for stator assembly of the Bacillus flagellar motor. Sci. Adv. 3:eaao4119.
Tribet, C., Audebert, R., Popot, J.-L. (1997) Stabilization of hydrophobic colloidal dispersions in water with amphiphilic
polymers: Application to integral membrane proteins. Langmuir 13:5570–5576.
Tribet, C., Diab, C., Dahmane, T., Zoonens, M., Popot, J.-L., Winnik, F.M. (2009) Thermodynamic characterization of
the exchange of detergents and amphipols at the surfaces of integral membrane proteins. Langmuir 25:12623–12634.
Tribet, C., Mills, D., Haider, M., Popot, J.-L. (1998) Scanning transmission electron microscopy study of the molecular
mass of amphipol/cytochrome b 6 f complexes. Biochimie 80:475–482.
Tsybovsky, Y., Orban, T., Molday, R.S., Taylor, D., Palczewski, K. (2013) Molecular organization and ATP-induced
conformational changes of ABCA4, the photoreceptor-specific ABC transporter. Structure 21:854–860.
Ubarretxena-Belandia, I., Stokes, D.L. (2010) Present and future of membrane protein structure determination by
electron crystallography. Adv. Protein Chem. Struct. Biol. 81:33–60.
Vahedi-Faridi, A., Jastrzebska, B., Palczewski, K., Engel, A. (2013) 3D imaging and quantitative analysis of small
solubilized membrane proteins and their complexes by transmission electron microscopy. Microscopy (Oxf)
62:95–107.
van Heel, M., Frank, J. (1981) Use of multivariate statistics in analysing the images of biological macromolecules.
Ultramicroscopy 6:187–194.
van Pee, K., Neuhaus, A., D’Imprima, E., Mills, D.J., Kühlbrandt, W., Yildiz, Ö. (2017) CryoEM structures of membrane
pore and prepore complex reveal cytolytic mechanism of pneumolysin. eLlife 6:e23644.
Venkatachalam, K., Montell, C. (2007) TRP channels. Annu. Rev. Biochem. 76:387–417.
Villa, E., Schaffer, M., Plitzko, J.M., Baumeister, W. (2013) Opening windows into the cell: focused-ion-beam milling
for cryo-electron tomography. Curr. Opin. Struct. Biol. 23:771–777.
Vinothkumar, K.R., Zhu, J., Hirst, J. (2014) Architecture of mammalian respiratory complex I. Nature 515:80–84.
Vinothkumar, K.R. (2015) Membrane protein structures without crystals, by single-particle electron cryomicroscopy.
Curr. Opin. Struct. Biol. 33:103–114.
Vinothkumar, K.R., Henderson, R. (2016) Single-particle electron cryomicroscopy: trends, issues and future perspective.
Q. Rev. Biophys. 49:e13.
Wang, Z., Fan, G., Hryc, C.F., Blaza, J.N., Serysheva, I.I., Schmid, M.F., Chiu, W., Luisi, B.F., Du, D. (2017) An
allosteric transport mechanism for the AcrAB-TolC multidrug efflux pump. eLife 6:e24905.
Wei, R., Wang, X., Zhang, Y., Mukherjee, S., Zhang, L., Chen, Q., Huang, X., Jing, S., Liu, C., Li, S., Wang, G., Xu, Y.,
Zhu, S., Williams, A.J., Sun, F., C.C. Y. (2016) Structural insights into Ca
2+ -activated long-range allosteric channel
gating of RyR1. Cell Res. 26:977–994.
Wilkens, S. (2000) F 1 F O -ATP synthase–stalking mind and imagination. J. Bioenerg. Biomembr. 32:333–339.
Wilkens, S., Capaldi, R.A. (1998a) Electron microscopic evidence of two stalks linking the F 1 and F O parts of the
Escherichia coli ATP synthase. Biochim. Biophys. Acta 1365:93–97.
Wilkens, S., Capaldi, R.A. (1998b) ATP synthase’s second stalk comes into focus. Nature 393:29.
Wilkens, S., Zhou, J., Nakayama, R., Dunn, S.D., Capaldi, R.A. (2000) Localization of the δ subunit in the Escherichia
coli F 1 F O -ATPsynthase by immuno-electron microscopy: The δ subunit binds on top of the F 1 . J. Mol. Biol.
295:387–391.
References
589