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ribosome. Proc. Natl. Acad. Sci. USA 107:17158–17163.
Cappuccio, J.A., Hinz, A.K., Kuhn, E.A., Fletcher, J.E., Arroyo, E.S., Henderson, P.T., Blanchette, C.D., Walsworth, V.
L., Corzett, M.H., Law, R.J., Pesavento, J.B., Segelke, B.W., Sulchek, T.A., Chromy, B.A., Katzen, F., Peterson, T.
C., Bench, G., Kudlicki, W., Hoeprich, P.D., Jr., Coleman, M.A. (2009) Cell-free expression for nanolipoprotein
particles: building a high-throughput membrane protein solubility platform. Methods Mol. Biol. 498:273–296.
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.
Chittum, H.S., Champney, W.S. (1994) Ribosomal protein gene sequence changes in erythromycin-resistant mutants of
Escherichia coli. J. Bact. 176:6192–6198.
Corin, K., Baaske, P., Ravel, D.B., Song, J., Brown, E., Wang, X., Wienken, C.J., Jerabek-Willemsen, M., Duhr, S., Luo,
Y., Braun, D., Zhang, S. (2011) Designer lipid-like peptides: a class of detergents for studying functional olfactory
receptors using commercial cell-free systems. PLoS ONE 6:e25067.
Dahmane, T., Rappaport, F., Popot, J.-L. (2013) Amphipol-assisted folding of bacteriorhodopsin in the presence and
absence of lipids. Functional consequences. Eur. Biophys. J. 42:85–101.
Diab, C., Tribet, C., Gohon, Y., Popot, J.-L., Winnik, F.M. (2007a) Complexation of integral membrane proteins by
phosphorylcholine-based amphipols. Biochim. Biophys. Acta 1768:2737–2747.
Diab, C., Winnik, F.M., Tribet, C. (2007b) Enthalpy of interaction and binding isotherms of non-ionic surfactants onto
micellar amphiphilic polymers (amphipols). Langmuir 23:3025–3035.
Ferrandez, Y., Dezi, M., Bosco, M., Urvoas, A., Valério, M., Le Bon, C., Giusti, F., Broutin, I., Durand, G., Polidori, A.,
Popot, J.-L., Picard, M., Minard, P. (2014) Amphipol-mediated screening of molecular orthoses specific for
membrane protein targets. J. Membr. Biol. 247:925–940.
Focke, P.J., Hein, C., Hoffmann, B., Matulef, K., Bernhard, F., Dötsch, V., Valiyaveetil, F.I. (2016) Combining in vitro
folding with cell-free protein synthesis for membrane protein expression. Biochemistry 55:4212–4219.
Ge, X., Xu, J. (2012) Cell-free protein synthesis as a promising expression system for recombinant proteins. Methods
Mol. Biol. 824:565–578.
Gohon, Y., Dahmane, T., Ruigrok, R., Schuck, P., Charvolin, D., Rappaport, F., Timmins, P., Engelman, D.M., Tribet,
C., Popot, J.-L., Ebel, C. (2008) Bacteriorhodopsin/amphipol complexes: structural and functional properties.
Biophys. J. 94:3523–3537.
Grisshammer, R., Tate, C.G. (1995) Overexpression of integral membrane proteins for structural studies. Quart. Rev.
Biophys. 28:315–422.
Guild, K., Zhang, Y., Stacy, R., Mundt, E., Benbow, S., Green, A., Myler, P.J. (2011) Wheat germ cell-free expression
system as a pathway to improve protein yield and solubility for the SSGCID pipeline. Acta Crystallogr. Sect. F Struct.
Biol. Cryst. Commun. 67:1027–1031.
Hein, C., Henrich, E., Orbán, E., Dötsch, V., Bernhard, F. (2014) Hydrophobic supplements in cell-free systems:
Designing artificial environments for membrane proteins. Engin. Life Sci. 14:365–379.
Henrich, E., Hein, C., Dötsch, V., Bernhard, F. (2015) Membrane protein production in Escherichia coli cell-free lysates.
FEBS Lett. 589:1713–1722.
Henrich, E., Peetz, O., Hein, C., LaGuerre, A., Hoffmann, B., Hoffmann, J., Dötsch, V., Bernhard, F., Morgner,
N. (2017) Analyzing native membrane protein assembly in nanodiscs by combined non-covalent mass spectrometry
and synthetic biology. eLife 6:e20954.
Hrmova, M., Stone, B.A., Fincher, G.B. (2010) High-yield production, refolding and molecular modelling of the
catalytic module of (1,3)-β-D-glucan (curdlan) synthase from Agrobacterium sp. Glycoconj. J. 27:461–476.
Huppa, J.B., Ploegh, H.L. (1997) In vitro translation and assembly of a complete T cell receptor-CD3 complex. J. Exp.
Med. 186:393–403.
Isaksson, L., Enberg, J., Neutze, R., Karlsson, B.G., Pedersen, A. (2012) Expression screening of membrane proteins
with cell-free protein synthesis. Protein Expr. Purif. 82:218–225.
Junge, F., Luh, L.M., Proverbio, D., Schäfer, B., Abele, R., Beyermann, M., Dötsch, V., Bernhard, F. (2010) Modulation
of G-protein coupled receptor sample quality by modified cell-free expression protocols: A case study of the human
endothelin A receptor. J. Struct. Biol. 172:94–106.
Kai, L., Roos, C., Haberstock, S., Proverbio, D., Ma, Y., Junge, F., Karbyshev, M., Dötsch, V., Bernhard, F. (2012)
Systems for the cell-free synthesis of proteins. Methods Mol. Biol. 800:201–215.
Kai, L., Orbán, E., Henrich, E., Proverbio, D., Dötsch, V., Bernhard, F. (2015) Co-translational stabilization of insoluble
proteins in cell-free expression systems. Methods Mol. Biol. 1258:125–143.
Kaiser, L., Graveland-Bikker, J., Steuerwald, D., Vanberghem, M., Herlihy, K., Zhang, S. (2008) Efficient cell-free
production of olfactory receptors: detergent optimization, structure, and ligand binding analyses. Proc. Natl. Acad.
Sci. USA 105:15726–15731.
References
377
ed., Membranes. Elsevier, Oxford:Academic Press, pp. 139–163.
Bulkley, D., Innis, A., Blaha, G., Steitz, T.A. (2010) Revisiting the structures of several antibiotics bound to the bacterial
ribosome. Proc. Natl. Acad. Sci. USA 107:17158–17163.
Cappuccio, J.A., Hinz, A.K., Kuhn, E.A., Fletcher, J.E., Arroyo, E.S., Henderson, P.T., Blanchette, C.D., Walsworth, V.
L., Corzett, M.H., Law, R.J., Pesavento, J.B., Segelke, B.W., Sulchek, T.A., Chromy, B.A., Katzen, F., Peterson, T.
C., Bench, G., Kudlicki, W., Hoeprich, P.D., Jr., Coleman, M.A. (2009) Cell-free expression for nanolipoprotein
particles: building a high-throughput membrane protein solubility platform. Methods Mol. Biol. 498:273–296.
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.
Chittum, H.S., Champney, W.S. (1994) Ribosomal protein gene sequence changes in erythromycin-resistant mutants of
Escherichia coli. J. Bact. 176:6192–6198.
Corin, K., Baaske, P., Ravel, D.B., Song, J., Brown, E., Wang, X., Wienken, C.J., Jerabek-Willemsen, M., Duhr, S., Luo,
Y., Braun, D., Zhang, S. (2011) Designer lipid-like peptides: a class of detergents for studying functional olfactory
receptors using commercial cell-free systems. PLoS ONE 6:e25067.
Dahmane, T., Rappaport, F., Popot, J.-L. (2013) Amphipol-assisted folding of bacteriorhodopsin in the presence and
absence of lipids. Functional consequences. Eur. Biophys. J. 42:85–101.
Diab, C., Tribet, C., Gohon, Y., Popot, J.-L., Winnik, F.M. (2007a) Complexation of integral membrane proteins by
phosphorylcholine-based amphipols. Biochim. Biophys. Acta 1768:2737–2747.
Diab, C., Winnik, F.M., Tribet, C. (2007b) Enthalpy of interaction and binding isotherms of non-ionic surfactants onto
micellar amphiphilic polymers (amphipols). Langmuir 23:3025–3035.
Ferrandez, Y., Dezi, M., Bosco, M., Urvoas, A., Valério, M., Le Bon, C., Giusti, F., Broutin, I., Durand, G., Polidori, A.,
Popot, J.-L., Picard, M., Minard, P. (2014) Amphipol-mediated screening of molecular orthoses specific for
membrane protein targets. J. Membr. Biol. 247:925–940.
Focke, P.J., Hein, C., Hoffmann, B., Matulef, K., Bernhard, F., Dötsch, V., Valiyaveetil, F.I. (2016) Combining in vitro
folding with cell-free protein synthesis for membrane protein expression. Biochemistry 55:4212–4219.
Ge, X., Xu, J. (2012) Cell-free protein synthesis as a promising expression system for recombinant proteins. Methods
Mol. Biol. 824:565–578.
Gohon, Y., Dahmane, T., Ruigrok, R., Schuck, P., Charvolin, D., Rappaport, F., Timmins, P., Engelman, D.M., Tribet,
C., Popot, J.-L., Ebel, C. (2008) Bacteriorhodopsin/amphipol complexes: structural and functional properties.
Biophys. J. 94:3523–3537.
Grisshammer, R., Tate, C.G. (1995) Overexpression of integral membrane proteins for structural studies. Quart. Rev.
Biophys. 28:315–422.
Guild, K., Zhang, Y., Stacy, R., Mundt, E., Benbow, S., Green, A., Myler, P.J. (2011) Wheat germ cell-free expression
system as a pathway to improve protein yield and solubility for the SSGCID pipeline. Acta Crystallogr. Sect. F Struct.
Biol. Cryst. Commun. 67:1027–1031.
Hein, C., Henrich, E., Orbán, E., Dötsch, V., Bernhard, F. (2014) Hydrophobic supplements in cell-free systems:
Designing artificial environments for membrane proteins. Engin. Life Sci. 14:365–379.
Henrich, E., Hein, C., Dötsch, V., Bernhard, F. (2015) Membrane protein production in Escherichia coli cell-free lysates.
FEBS Lett. 589:1713–1722.
Henrich, E., Peetz, O., Hein, C., LaGuerre, A., Hoffmann, B., Hoffmann, J., Dötsch, V., Bernhard, F., Morgner,
N. (2017) Analyzing native membrane protein assembly in nanodiscs by combined non-covalent mass spectrometry
and synthetic biology. eLife 6:e20954.
Hrmova, M., Stone, B.A., Fincher, G.B. (2010) High-yield production, refolding and molecular modelling of the
catalytic module of (1,3)-β-D-glucan (curdlan) synthase from Agrobacterium sp. Glycoconj. J. 27:461–476.
Huppa, J.B., Ploegh, H.L. (1997) In vitro translation and assembly of a complete T cell receptor-CD3 complex. J. Exp.
Med. 186:393–403.
Isaksson, L., Enberg, J., Neutze, R., Karlsson, B.G., Pedersen, A. (2012) Expression screening of membrane proteins
with cell-free protein synthesis. Protein Expr. Purif. 82:218–225.
Junge, F., Luh, L.M., Proverbio, D., Schäfer, B., Abele, R., Beyermann, M., Dötsch, V., Bernhard, F. (2010) Modulation
of G-protein coupled receptor sample quality by modified cell-free expression protocols: A case study of the human
endothelin A receptor. J. Struct. Biol. 172:94–106.
Kai, L., Roos, C., Haberstock, S., Proverbio, D., Ma, Y., Junge, F., Karbyshev, M., Dötsch, V., Bernhard, F. (2012)
Systems for the cell-free synthesis of proteins. Methods Mol. Biol. 800:201–215.
Kai, L., Orbán, E., Henrich, E., Proverbio, D., Dötsch, V., Bernhard, F. (2015) Co-translational stabilization of insoluble
proteins in cell-free expression systems. Methods Mol. Biol. 1258:125–143.
Kaiser, L., Graveland-Bikker, J., Steuerwald, D., Vanberghem, M., Herlihy, K., Zhang, S. (2008) Efficient cell-free
production of olfactory receptors: detergent optimization, structure, and ligand binding analyses. Proc. Natl. Acad.
Sci. USA 105:15726–15731.
References
377