References
Agah, S., Faham, S. (2012) Crystallization of membrane proteins in bicelles. Methods Mol. Biol. 914:3–16.
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.
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.
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.
Berger, B.W., Gendron, C.M., Robinson, C.R., Kaler, E.W., Lenhoff, A.M. (2005) The role of protein and surfactant
interactions in membrane-protein crystallization. Acta Crystallogr. D 61:724–730.
Berry, E.A., Guergova-Kuras, M., Huang, L.-S., Crofts, A.R. (2000) Structure and function of cytochrome bc 1
complexes. Annu. Rev. Biochem. 69:1005–1075.
Berry, E.A., Huang, L.-S., DeRose, V. (1991) Ubiquinol-cytochrome c oxidoreductase from higher plants. Isolation and
characterization of the bc 1 complex from potato tuber mitochondria. J. Biol. Chem. 266:9064–9077.
Binz, H.K., Stumpp, M.T., Forrer, P., Amstutz, P., Plückthun, A. (2003) Designing repeat proteins: well-expressed,
soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. J. Mol. Biol.
332:489–503.
Boersma, Y.L., Plückthun, A. (2011) DARPins and other repeat protein scaffolds: advances in engineering and
applications. Curr. Opin. Biotechnol. 22:849–857.
Bogorodskiy, A., Frolov, F., Mishin, A., Round, E., Polovinkin, V., Cherezov, V., Gordeliy, V., Büldt, G., Gensch, T.,
Borshchevskiy’, V. (2015) Nucleation and growth of membrane protein crystals in meso–A fluorescence microscopy
study. Cryst. Growth Des. 15:5656–5660.
Borshchevskiy, V.I., Round, E.S., Popov, A.N., Büldt, G., Gordeliy, V.I. (2011) X-ray-radiation-induced changes in
bacteriorhodopsin structure. J. Mol. Biol. 409:813–825.
Boutet, S., Lomb, L., Williams, G.J., Barends, T.R.M., Aquila, A., Doak, R.B., Weierstall, U., DePonte, D.P.,
Steinbrener, J., Shoeman, R.L., Messerschmidt, M., Barty, A., White, T.A., Kassemeyer, S., Kirian, R.A., Seibert,
M.M., Montanez, P.A., Kenney, C., Herbst, R., Hart, P., Pines, J., Haller, G., Gruner, S.M., Philipp, H.T., Tate, M.
W., Hromalik, M., Koerner, L.J., Bakel, N., Morse, J., Ghonsalves, W., Arnlund, D., Bogan, M.J., Caleman, C.,
Fromme, R., Hampton, C.Y., Hunter, M.S., Johansson, L.C., Katona, G., Kupitz, C., Liang, M., Martin, A.V., Nass,
K., Redecke, L., Stellato, F., Timneanu, N., Wang, D., Zatsepin, N.A., Schafer, D., Defever, J., Neutze, R., Fromme,
P., Spence, J.C.H., Chapman, H.N., Schlichting, I. (2012) High-resolution protein structure determination by serial
femtosecond crystallography. Science 337:362–364.
Bowie, J.U. (2001) Stabilizing membrane proteins. Curr. Opin. Struct. Biol. 11:397–402.
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.
Broecker, J., Eger, B.T., Ernst, O.P. (2017) Crystallogenesis of membrane proteins mediated by polymer-bounded lipid
nanodiscs. Structure 25:384–392.
Caffrey, M. (2003) Membrane protein crystallization. J. Struct. Biol. 142:108–132.
Caffrey, M. (2009) Crystallizing membrane proteins for structure determination: use of lipidic mesophases. Annu. Rev.
Biophys. 38:29–51.
Caffrey, M. (2011) Crystallizing membrane proteins for structure-function studies using lipidic mesophases. Biochem.
Soc. Trans. 39:725–732.
Caffrey, M. (2015) A comprehensive review of the lipid cubic phase or in meso method for crystallizing membrane and
soluble proteins and complexes. Acta Crystallogr. F 71:3–18.
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.
Chae, P.S., Rasmussen, S.G.F., Rana, R., Gotfryd, K., Chandra, R., Goren, M.A., Kruse, A.C., Nurva, S., Loland, C.J.,
Pierre, Y., Drew, D., Popot, J.-L., Picot, D., Fox, B.G., Guan, L., Gether, U., Byrne, B., Kobilka, B.K., Gellman,
S.H. (2010) Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of
membrane proteins. Nat. Methods 7:1003–1008.
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.
Chapman, H.N., Fromme, P., Barty, A., White, T.A., Kirian, R.A., Aquila, A., Hunter, M.S., Schulz, J., DePonte, D.P.,
Weierstall, U., Doak, R.B., Maia, F.R.N.C., Martin, A.V., Schlichting, I., Lomb, L., Coppola, N., Shoeman, R.L.,
Epp, S.W., Hartmann, R., Rolles, D., Rudenko, A., Foucar, L., Kimmel, N., Weidenspointner, G., Holl, P., Liang, M.,
References
525
Agah, S., Faham, S. (2012) Crystallization of membrane proteins in bicelles. Methods Mol. Biol. 914:3–16.
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.
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.
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.
Berger, B.W., Gendron, C.M., Robinson, C.R., Kaler, E.W., Lenhoff, A.M. (2005) The role of protein and surfactant
interactions in membrane-protein crystallization. Acta Crystallogr. D 61:724–730.
Berry, E.A., Guergova-Kuras, M., Huang, L.-S., Crofts, A.R. (2000) Structure and function of cytochrome bc 1
complexes. Annu. Rev. Biochem. 69:1005–1075.
Berry, E.A., Huang, L.-S., DeRose, V. (1991) Ubiquinol-cytochrome c oxidoreductase from higher plants. Isolation and
characterization of the bc 1 complex from potato tuber mitochondria. J. Biol. Chem. 266:9064–9077.
Binz, H.K., Stumpp, M.T., Forrer, P., Amstutz, P., Plückthun, A. (2003) Designing repeat proteins: well-expressed,
soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. J. Mol. Biol.
332:489–503.
Boersma, Y.L., Plückthun, A. (2011) DARPins and other repeat protein scaffolds: advances in engineering and
applications. Curr. Opin. Biotechnol. 22:849–857.
Bogorodskiy, A., Frolov, F., Mishin, A., Round, E., Polovinkin, V., Cherezov, V., Gordeliy, V., Büldt, G., Gensch, T.,
Borshchevskiy’, V. (2015) Nucleation and growth of membrane protein crystals in meso–A fluorescence microscopy
study. Cryst. Growth Des. 15:5656–5660.
Borshchevskiy, V.I., Round, E.S., Popov, A.N., Büldt, G., Gordeliy, V.I. (2011) X-ray-radiation-induced changes in
bacteriorhodopsin structure. J. Mol. Biol. 409:813–825.
Boutet, S., Lomb, L., Williams, G.J., Barends, T.R.M., Aquila, A., Doak, R.B., Weierstall, U., DePonte, D.P.,
Steinbrener, J., Shoeman, R.L., Messerschmidt, M., Barty, A., White, T.A., Kassemeyer, S., Kirian, R.A., Seibert,
M.M., Montanez, P.A., Kenney, C., Herbst, R., Hart, P., Pines, J., Haller, G., Gruner, S.M., Philipp, H.T., Tate, M.
W., Hromalik, M., Koerner, L.J., Bakel, N., Morse, J., Ghonsalves, W., Arnlund, D., Bogan, M.J., Caleman, C.,
Fromme, R., Hampton, C.Y., Hunter, M.S., Johansson, L.C., Katona, G., Kupitz, C., Liang, M., Martin, A.V., Nass,
K., Redecke, L., Stellato, F., Timneanu, N., Wang, D., Zatsepin, N.A., Schafer, D., Defever, J., Neutze, R., Fromme,
P., Spence, J.C.H., Chapman, H.N., Schlichting, I. (2012) High-resolution protein structure determination by serial
femtosecond crystallography. Science 337:362–364.
Bowie, J.U. (2001) Stabilizing membrane proteins. Curr. Opin. Struct. Biol. 11:397–402.
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.
Broecker, J., Eger, B.T., Ernst, O.P. (2017) Crystallogenesis of membrane proteins mediated by polymer-bounded lipid
nanodiscs. Structure 25:384–392.
Caffrey, M. (2003) Membrane protein crystallization. J. Struct. Biol. 142:108–132.
Caffrey, M. (2009) Crystallizing membrane proteins for structure determination: use of lipidic mesophases. Annu. Rev.
Biophys. 38:29–51.
Caffrey, M. (2011) Crystallizing membrane proteins for structure-function studies using lipidic mesophases. Biochem.
Soc. Trans. 39:725–732.
Caffrey, M. (2015) A comprehensive review of the lipid cubic phase or in meso method for crystallizing membrane and
soluble proteins and complexes. Acta Crystallogr. F 71:3–18.
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.
Chae, P.S., Rasmussen, S.G.F., Rana, R., Gotfryd, K., Chandra, R., Goren, M.A., Kruse, A.C., Nurva, S., Loland, C.J.,
Pierre, Y., Drew, D., Popot, J.-L., Picot, D., Fox, B.G., Guan, L., Gether, U., Byrne, B., Kobilka, B.K., Gellman,
S.H. (2010) Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of
membrane proteins. Nat. Methods 7:1003–1008.
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.
Chapman, H.N., Fromme, P., Barty, A., White, T.A., Kirian, R.A., Aquila, A., Hunter, M.S., Schulz, J., DePonte, D.P.,
Weierstall, U., Doak, R.B., Maia, F.R.N.C., Martin, A.V., Schlichting, I., Lomb, L., Coppola, N., Shoeman, R.L.,
Epp, S.W., Hartmann, R., Rolles, D., Rudenko, A., Foucar, L., Kimmel, N., Weidenspointner, G., Holl, P., Liang, M.,
References
525