Nikolaev, M., Round, E., Gushchin, I., Polovinkin, V., Balandin, T., Kuzmichev, P., Shevchenko, V., Borshchevskiy,
V., Kuklin, A., Round, A., Bernhard, F., Willbold, D., Büldt, G., Gordeliy, V. (2017) Integral membrane proteins can
be crystallized directly from nanodiscs. Cryst. Growth Des. 17:945–948.
Nollert, P. (2004) Lipidic cubic phases as matrices for membrane protein crystallization. Methods 34:348–353.
Nollert, P. (2005) Membrane protein crystallization in amphiphile phases: practical and theoretical considerations. Prog.
Biophys. Mol. Biol. 88:339–357.
Ostermeier, C., Harrenga, A., Ermler, U., Michel, H. (1997) Structure at 2.7 Å resolution of the Paracoccus denitrificans
two-subunit cytochrome c oxidase complexed with an antibody F v fragment. Proc. Natl. Acad. Sci. USA
94:10547–10553.
Ostermeier, C., Iwata, S., Ludwig, B., Michel, H. (1995) F v fragment-mediated crystallization of the membrane protein
bacterial cytochrome c oxidase. Nature Struct. Biol. 2:842–846.
Ostermeier, C., Michel, H. (1997) Crystallization of membrane proteins. Curr. Opin. Struct. Biol. 7:697–701.
Parker, J.L., Newstead, S. (2012) Current trends in α-helical membrane protein crystallization: An update. Prot. Sci.
21:1358–1365.
Pebay-Peyroula, E., Rummel, G., Rosenbusch, J.P., Landau, E. (1997) X-ray structure of bacteriorhodopsin at 2.5 Å from
microcrystals grown in lipidic cubic phases. Science 277:1676–1881.
Perlmutter, J.D., Popot, J.-L., Sachs, J.N. (2014) Molecular dynamics simulations of a membrane protein/amphipol
complex. J. Membr. Biol. 247:883–895.
Plückthun, A. (2015) Designed ankyrin repeat proteins (DARPins): binding proteins for research, diagnostics, and
therapy. Annu. Rev. Pharmacol. Toxicol. 55:489–511.
Pocanschi, C.L., Dahmane, T., Gohon, Y., Rappaport, F., Apell, H.-J., Kleinschmidt, J.H., Popot, J.-L. (2006) Amphipathic polymers: tools to fold integral membrane proteins to their active form. Biochemistry 45:13954–13961.
Polovinkin, V., Gushchin, I., Balandin, T., Chervakov, P., Round, E., Shevchenko, V., Popov, A., Borshchevskiy, V.,
Popot, J.-L., Gordeliy, V. (2014) High-resolution structure of a membrane protein transferred from amphipol to a
lipidic mesophase. J. Membr. Biol. 247:997–1004.
Popot, J.-L. (2014) Folding membrane proteins in vitro: A table and some comments. Arch. Biochem. Biophys.
564:314–326.
Popot, J.-L., Berry, E.A., Charvolin, D., Creuzenet, C., Ebel, C., Engelman, D.M., Flötenmeyer, M., Giusti, F., Gohon,
Y., Hervé, P., Hong, Q., Lakey, J.H., Leonard, K., Shuman, H.A., Timmins, P., Warschawski, D.E., Zito, F.,
Zoonens, M., Pucci, B., Tribet, C. (2003) Amphipols: polymeric surfactants for membrane biology research. Cell.
Mol. Life Sci. 60:1559–1574.
Poulos, S., Morgan, J.L., Zimmer, J., Faham, S. (2015) Bicelles coming of age: an empirical approach to bicelle
crystallization. Meth. Enzymol. 557:393–416.
Prata, C., Giusti, F., Gohon, Y., Pucci, B., Popot, J.-L., Tribet, C. (2001) Non-ionic amphiphilic polymers derived from
tris(hydroxymethyl)-acrylamidomethane keep membrane proteins soluble and native in the absence of detergent.
Biopolymers 56:77–84.
Privé, G.G. (2007) Detergents for the stabilization and crystallization of membrane proteins. Methods 41:388–397.
Qiu, H., Caffrey, M. (2000) Phase diagram of the monoolein/water system: metastability and equilibrium aspects.
Biomaterials 21:223–234.
Rasmussen, S.G., Choi, H.J., Rosenbaum, D.M., Kobilka, T.S., Thian, F.S., Edwards, P.C., Burghammer, M., Ratnala,
V.R., Sanishvili, R., Fischetti, R.F., Schertler, G.F., Weis, W.I., Kobilka, B.K. (2007) Crystal structure of the human
β 2 adrenergic G protein-coupled receptor. Nature 450:383–387.
Rasmussen, S.G.F., Choi, H.-J., Fung, J.J., Pardon, E., Casarosa, P., Chae, P.S., DeVree, B.T., Rosenbaum, D.M., Thian,
F.S., Kobilka, T.S., Schnapp, A., Konetzki, I., Sunahara, R.K., Gellman, S.H., Pautsch, A., Steyaert, J., Weis, W.I.,
Kobilka, B.K. (2011) Structure of a nanobody-stabilized active state of the β 2 adrenoceptor. Nature 469:175–180.
Rosenbaum, D.M., Cherezov, V., Hanson, M.A., Rasmussen, S.G., Thian, F.S., Kobilka, T.S., Choi, H.J., Yao, X.J.,
Weis, W.I., Stevens, R.C., Kobilka, B.K. (2007) GPCR engineering yields high-resolution structural insights into β 2 -
adrenergic receptor function. Science 318:1266–1273.
Roth, M., Lewitt-Bentley, A., Michel, H., Deisenhofer, J., Huber, R., Oesterhelt, D. (1989) Detergent structure in crystals
of a bacterial photosynthetic reaction center. Nature 340:659–662.
Rummel, G., Hardmeyer, A., Widmer, C., Chiu, M.L., Nollert, P., Locher, K.P., Pedruzzi, I.I., Landau, E.M.,
Rosenbusch, J.P. (1998) Lipidic cubic phases: new matrices for the three-dimensional crystallization of membrane
proteins. J. Struct. Biol. 121:82–91.
Sadaf, A., Cho, K.H., Byrne, B., Chae, P.S. (2015) Amphipathic agents for membrane protein study. Meth. Enzymol.
557:57–94.
Sarkar, C.A., Dodevski, I., Kenig, M., Dudli, S., Mohr, A., Hermans, E., Plückthun, A. (2008) Directed evolution of a G
protein-coupled receptor for expression, stability, and binding selectivity. Proc. Natl. Acad. Sci. USA
105:14808–14813.
References
529
V., Kuklin, A., Round, A., Bernhard, F., Willbold, D., Büldt, G., Gordeliy, V. (2017) Integral membrane proteins can
be crystallized directly from nanodiscs. Cryst. Growth Des. 17:945–948.
Nollert, P. (2004) Lipidic cubic phases as matrices for membrane protein crystallization. Methods 34:348–353.
Nollert, P. (2005) Membrane protein crystallization in amphiphile phases: practical and theoretical considerations. Prog.
Biophys. Mol. Biol. 88:339–357.
Ostermeier, C., Harrenga, A., Ermler, U., Michel, H. (1997) Structure at 2.7 Å resolution of the Paracoccus denitrificans
two-subunit cytochrome c oxidase complexed with an antibody F v fragment. Proc. Natl. Acad. Sci. USA
94:10547–10553.
Ostermeier, C., Iwata, S., Ludwig, B., Michel, H. (1995) F v fragment-mediated crystallization of the membrane protein
bacterial cytochrome c oxidase. Nature Struct. Biol. 2:842–846.
Ostermeier, C., Michel, H. (1997) Crystallization of membrane proteins. Curr. Opin. Struct. Biol. 7:697–701.
Parker, J.L., Newstead, S. (2012) Current trends in α-helical membrane protein crystallization: An update. Prot. Sci.
21:1358–1365.
Pebay-Peyroula, E., Rummel, G., Rosenbusch, J.P., Landau, E. (1997) X-ray structure of bacteriorhodopsin at 2.5 Å from
microcrystals grown in lipidic cubic phases. Science 277:1676–1881.
Perlmutter, J.D., Popot, J.-L., Sachs, J.N. (2014) Molecular dynamics simulations of a membrane protein/amphipol
complex. J. Membr. Biol. 247:883–895.
Plückthun, A. (2015) Designed ankyrin repeat proteins (DARPins): binding proteins for research, diagnostics, and
therapy. Annu. Rev. Pharmacol. Toxicol. 55:489–511.
Pocanschi, C.L., Dahmane, T., Gohon, Y., Rappaport, F., Apell, H.-J., Kleinschmidt, J.H., Popot, J.-L. (2006) Amphipathic polymers: tools to fold integral membrane proteins to their active form. Biochemistry 45:13954–13961.
Polovinkin, V., Gushchin, I., Balandin, T., Chervakov, P., Round, E., Shevchenko, V., Popov, A., Borshchevskiy, V.,
Popot, J.-L., Gordeliy, V. (2014) High-resolution structure of a membrane protein transferred from amphipol to a
lipidic mesophase. J. Membr. Biol. 247:997–1004.
Popot, J.-L. (2014) Folding membrane proteins in vitro: A table and some comments. Arch. Biochem. Biophys.
564:314–326.
Popot, J.-L., Berry, E.A., Charvolin, D., Creuzenet, C., Ebel, C., Engelman, D.M., Flötenmeyer, M., Giusti, F., Gohon,
Y., Hervé, P., Hong, Q., Lakey, J.H., Leonard, K., Shuman, H.A., Timmins, P., Warschawski, D.E., Zito, F.,
Zoonens, M., Pucci, B., Tribet, C. (2003) Amphipols: polymeric surfactants for membrane biology research. Cell.
Mol. Life Sci. 60:1559–1574.
Poulos, S., Morgan, J.L., Zimmer, J., Faham, S. (2015) Bicelles coming of age: an empirical approach to bicelle
crystallization. Meth. Enzymol. 557:393–416.
Prata, C., Giusti, F., Gohon, Y., Pucci, B., Popot, J.-L., Tribet, C. (2001) Non-ionic amphiphilic polymers derived from
tris(hydroxymethyl)-acrylamidomethane keep membrane proteins soluble and native in the absence of detergent.
Biopolymers 56:77–84.
Privé, G.G. (2007) Detergents for the stabilization and crystallization of membrane proteins. Methods 41:388–397.
Qiu, H., Caffrey, M. (2000) Phase diagram of the monoolein/water system: metastability and equilibrium aspects.
Biomaterials 21:223–234.
Rasmussen, S.G., Choi, H.J., Rosenbaum, D.M., Kobilka, T.S., Thian, F.S., Edwards, P.C., Burghammer, M., Ratnala,
V.R., Sanishvili, R., Fischetti, R.F., Schertler, G.F., Weis, W.I., Kobilka, B.K. (2007) Crystal structure of the human
β 2 adrenergic G protein-coupled receptor. Nature 450:383–387.
Rasmussen, S.G.F., Choi, H.-J., Fung, J.J., Pardon, E., Casarosa, P., Chae, P.S., DeVree, B.T., Rosenbaum, D.M., Thian,
F.S., Kobilka, T.S., Schnapp, A., Konetzki, I., Sunahara, R.K., Gellman, S.H., Pautsch, A., Steyaert, J., Weis, W.I.,
Kobilka, B.K. (2011) Structure of a nanobody-stabilized active state of the β 2 adrenoceptor. Nature 469:175–180.
Rosenbaum, D.M., Cherezov, V., Hanson, M.A., Rasmussen, S.G., Thian, F.S., Kobilka, T.S., Choi, H.J., Yao, X.J.,
Weis, W.I., Stevens, R.C., Kobilka, B.K. (2007) GPCR engineering yields high-resolution structural insights into β 2 -
adrenergic receptor function. Science 318:1266–1273.
Roth, M., Lewitt-Bentley, A., Michel, H., Deisenhofer, J., Huber, R., Oesterhelt, D. (1989) Detergent structure in crystals
of a bacterial photosynthetic reaction center. Nature 340:659–662.
Rummel, G., Hardmeyer, A., Widmer, C., Chiu, M.L., Nollert, P., Locher, K.P., Pedruzzi, I.I., Landau, E.M.,
Rosenbusch, J.P. (1998) Lipidic cubic phases: new matrices for the three-dimensional crystallization of membrane
proteins. J. Struct. Biol. 121:82–91.
Sadaf, A., Cho, K.H., Byrne, B., Chae, P.S. (2015) Amphipathic agents for membrane protein study. Meth. Enzymol.
557:57–94.
Sarkar, C.A., Dodevski, I., Kenig, M., Dudli, S., Mohr, A., Hermans, E., Plückthun, A. (2008) Directed evolution of a G
protein-coupled receptor for expression, stability, and binding selectivity. Proc. Natl. Acad. Sci. USA
105:14808–14813.
References
529