메뉴 건너뛰기




Volumn 4, Issue 5, 2009, Pages 706-731

Crystallizing membrane proteins using lipidic mesophases

Author keywords

[No Author keywords available]

Indexed keywords

BETA 2 ADRENERGIC RECEPTOR; BTUB PROTEIN, E COLI; CARRIER PROTEIN; ESCHERICHIA COLI PROTEIN; G PROTEIN COUPLED RECEPTOR; MEMBRANE LIPID; MEMBRANE PROTEIN; OPCA PROTEIN, NEISSERIA MENINGITIDIS; OUTER MEMBRANE PROTEIN;

EID: 67649392795     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2009.31     Document Type: Article
Times cited : (552)

References (57)
  • 3
    • 0037391107 scopus 로고    scopus 로고
    • Membrane protein crystallization
    • Caffrey, M. Membrane protein crystallization. J. Struct. Biol. 142, 108-132 (2003).
    • (2003) J. Struct. Biol , vol.142 , pp. 108-132
    • Caffrey, M.1
  • 4
    • 4344579363 scopus 로고    scopus 로고
    • A pedestrian guide to membrane protein crystallization
    • Wiener, M.C. A pedestrian guide to membrane protein crystallization. Methods 34, 364-372 (2004).
    • (2004) Methods , vol.34 , pp. 364-372
    • Wiener, M.C.1
  • 5
    • 0028079046 scopus 로고
    • Crystallization of membrane proteins forX-ray analysis. Methods
    • Sutton, B.J. & Sohi, M.K. Crystallization of membrane proteins forX-ray analysis. Methods Mol. Biol. 27, 1-18 (1994).
    • (1994) Mol. Biol , vol.27 , pp. 1-18
    • Sutton, B.J.1    Sohi, M.K.2
  • 6
    • 3042821641 scopus 로고    scopus 로고
    • Crystallization of Photosystem I
    • (ed. Iwata, S., International University Line, San Diego
    • Fromme, P Crystallization of Photosystem I. In Methods and Results in Crystallization of Membrane Proteins (ed. Iwata, S.) 145-174 (International University Line, San Diego, 2003).
    • (2003) Methods and Results in Crystallization of Membrane Proteins , pp. 145-174
    • Fromme, P.1
  • 7
    • 49649112228 scopus 로고    scopus 로고
    • Protein crystallization in restricted geometry: Advancing old ideas for modern times in structural proteomics
    • Ng, J.D., Stevens, R.C. & Kuhn, P. Protein crystallization in restricted geometry: advancing old ideas for modern times in structural proteomics. Methods Mol. Biol. 426, 363-376 (2008).
    • (2008) Methods Mol. Biol , vol.426 , pp. 363-376
    • Ng, J.D.1    Stevens, R.C.2    Kuhn, P.3
  • 8
    • 0037392851 scopus 로고    scopus 로고
    • Protein crystallization by capillary counterdiffusion for applied crystallographic structure determination
    • Ng, J.D., Gavira, J.A. & Garcia-Ruiz, J.M. Protein crystallization by capillary counterdiffusion for applied crystallographic structure determination. J. Struct. Biol. 142, 218-231 (2003).
    • (2003) J. Struct. Biol , vol.142 , pp. 218-231
    • Ng, J.D.1    Gavira, J.A.2    Garcia-Ruiz, J.M.3
  • 9
    • 0037706939 scopus 로고    scopus 로고
    • Compatibility of detergents with the microbatch-under-oil crystallization method
    • Loll, P.J., Tretiakova, A. & Soderblom, E. Compatibility of detergents with the microbatch-under-oil crystallization method. Acta Crystallogr. D Biol. Crystallogr. 59, 1114-1116 (2003).
    • (2003) Acta Crystallogr. D Biol. Crystallogr , vol.59 , pp. 1114-1116
    • Loll, P.J.1    Tretiakova, A.2    Soderblom, E.3
  • 10
    • 4344648879 scopus 로고    scopus 로고
    • Crystallization of Membrane Proteins in Oils
    • (ed. Iwata, S., International University Line, San Diego
    • Chayen, N.E. Crystallization of Membrane Proteins in Oils. In Methods and Results in Ciystallization of Membrane Proteins (ed. Iwata, S.) 131-140 (International University Line, San Diego, 2003).
    • (2003) Methods and Results in Ciystallization of Membrane Proteins , pp. 131-140
    • Chayen, N.E.1
  • 12
    • 0036301007 scopus 로고    scopus 로고
    • Bicelle crystallization: A new method for crystallizing membrane proteinsyields a monomeric bacteriorhodopsin structure
    • Faham, S. & Bowie, J.U. Bicelle crystallization: a new method for crystallizing membrane proteinsyields a monomeric bacteriorhodopsin structure. J. Mol. Biol. 316, 1-6 (2002).
    • (2002) J. Mol. Biol , vol.316 , pp. 1-6
    • Faham, S.1    Bowie, J.U.2
  • 13
    • 0032561127 scopus 로고    scopus 로고
    • Anovelthree-dimensional crystal ofbacteriorhodopsinobtained by successive fusion of the vesicular assemblies
    • Takeda, K. et al. Anovelthree-dimensional crystal ofbacteriorhodopsinobtained by successive fusion of the vesicular assemblies. J. Mol. Biol. 283, 463-474 (1998).
    • (1998) J. Mol. Biol , vol.283 , pp. 463-474
    • Takeda, K.1
  • 14
    • 0033992338 scopus 로고    scopus 로고
    • The phase diagram of the monoolein/water system: Metastability and equilibrium aspects
    • Qiu, H. & Caffrey, M. The phase diagram of the monoolein/water system: metastability and equilibrium aspects. Biomaterials 21, 223-234 (2000).
    • (2000) Biomaterials , vol.21 , pp. 223-234
    • Qiu, H.1    Caffrey, M.2
  • 15
    • 0002787636 scopus 로고
    • X-ray diffraction studies of lipid-water systems
    • (ed. Chapman, D., Academic Press, London
    • Luzzati, V. X-ray diffraction studies of lipid-water systems. In Biological Membranes, Physical Fact and Function Vol. 1, (ed. Chapman, D.) 71-123 (Academic Press, London, 1968).
    • (1968) Biological Membranes, Physical Fact and Function , vol.1 , pp. 71-123
    • Luzzati, V.1
  • 16
    • 0015788231 scopus 로고
    • The phase behavior of monogalactosyl, digalactosyl, and sulphoquinovosyl diglycerides
    • Shipley, G.G., Green, J.P. & Nichols, B.W. The phase behavior of monogalactosyl, digalactosyl, and sulphoquinovosyl diglycerides. Biochim. Biophys. Acta 311, 531-544 (1973).
    • (1973) Biochim. Biophys. Acta , vol.311 , pp. 531-544
    • Shipley, G.G.1    Green, J.P.2    Nichols, B.W.3
  • 17
    • 84934436616 scopus 로고    scopus 로고
    • Protocol to enrich and analyze plasma membrane proteins from frozen tissues
    • Wisniewski, J.R. Protocol to enrich and analyze plasma membrane proteins from frozen tissues. Methods Mol. Biol. 432, 175-183 (2008).
    • (2008) Methods Mol. Biol , vol.432 , pp. 175-183
    • Wisniewski, J.R.1
  • 18
    • 1842841323 scopus 로고    scopus 로고
    • Immobilized metal-ion affinity chromatography
    • Yip, T.T. & Hutchens, T.W. Immobilized metal-ion affinity chromatography. Methods Mol. Biol. 244, 179-190 (2004).
    • (2004) Methods Mol. Biol , vol.244 , pp. 179-190
    • Yip, T.T.1    Hutchens, T.W.2
  • 19
    • 1842841330 scopus 로고    scopus 로고
    • Ion-exchange chromatography
    • Selkirk, C. Ion-exchange chromatography. Methods Mol. Biol. 244, 125-131 (2004).
    • (2004) Methods Mol. Biol , vol.244 , pp. 125-131
    • Selkirk, C.1
  • 20
    • 1842863239 scopus 로고    scopus 로고
    • Size-exclusion chromatography
    • Cutler, P. Size-exclusion chromatography. Methods Mol. Biol. 244, 239-252 (2004).
    • (2004) Methods Mol. Biol , vol.244 , pp. 239-252
    • Cutler, P.1
  • 21
    • 0029992660 scopus 로고    scopus 로고
    • Lipidic cubic phases: A novel concept for the crystallization ofmembrane proteins
    • Landau, E.M. & Rosenbusch, J.P. Lipidic cubic phases: a novel concept for the crystallization ofmembrane proteins. Proc. Natl. Acad. Sci. USA 93,14532-14535 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14532-14535
    • Landau, E.M.1    Rosenbusch, J.P.2
  • 22
    • 33645054559 scopus 로고    scopus 로고
    • Room to move: Crystallizing membrane proteins in swollen lipidic mesophases
    • Cherezov, V., Clogston, J., Papiz, M.Z. & Caffrey, M. Room to move: crystallizing membrane proteins in swollen lipidic mesophases. J. Mol. Biol. 357, 1605-1618 (2006).
    • (2006) J. Mol. Biol , vol.357 , pp. 1605-1618
    • Cherezov, V.1    Clogston, J.2    Papiz, M.Z.3    Caffrey, M.4
  • 23
    • 33750965918 scopus 로고    scopus 로고
    • In meso structure ofthe cobalamin transporter, BtuB, at 1.95 A resolution
    • Cherezov, V. et al. In meso structure ofthe cobalamin transporter, BtuB, at 1.95 A resolution. J. Mol. Biol. 364, 716-734 (2006).
    • (2006) J. Mol. Biol , vol.364 , pp. 716-734
    • Cherezov, V.1
  • 24
    • 40549083360 scopus 로고    scopus 로고
    • In meso crystal structure and docking simulations suggest an alternative proteoglycan binding site in the OpcA outer membrane adhesin
    • Cherezov, V. et al. In meso crystal structure and docking simulations suggest an alternative proteoglycan binding site in the OpcA outer membrane adhesin. Proteins 71, 24-34 (2008).
    • (2008) Proteins , vol.71 , pp. 24-34
    • Cherezov, V.1
  • 25
    • 36448995359 scopus 로고    scopus 로고
    • High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor
    • Cherezov, V. et al. High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor. Science 318, 1258-1265 (2007).
    • (2007) Science , vol.318 , pp. 1258-1265
    • Cherezov, V.1
  • 26
    • 56749103466 scopus 로고    scopus 로고
    • The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist
    • Jaakola, V.P. et al. The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist. Science 322, 1211-1217 (2008).
    • (2008) Science , vol.322 , pp. 1211-1217
    • Jaakola, V.P.1
  • 27
    • 0242367561 scopus 로고    scopus 로고
    • Nano-volume plates with excellent opticalproperties for fast, inexpensive crystallization screening of membrane proteins
    • Cherezov, V. & Caffrey, M. Nano-volume plates with excellent opticalproperties for fast, inexpensive crystallization screening of membrane proteins. J. Appl. Cryst. 36, 1372-1377 (2003).
    • (2003) J. Appl. Cryst , vol.36 , pp. 1372-1377
    • Cherezov, V.1    Caffrey, M.2
  • 29
    • 33746421548 scopus 로고    scopus 로고
    • Picolitre-scale crystallization of membrane proteins
    • Cherezov, V. & Caffrey, M. Picolitre-scale crystallization of membrane proteins. J. Appl. Cryst. 39, 604-606 (2006).
    • (2006) J. Appl. Cryst , vol.39 , pp. 604-606
    • Cherezov, V.1    Caffrey, M.2
  • 30
    • 16844384800 scopus 로고    scopus 로고
    • A simple and inexpensive nanoliter-volume dispenser for highly viscous materials used in membrane protein crystallization
    • Cherezov, V. & Caffrey, M. A simple and inexpensive nanoliter-volume dispenser for highly viscous materials used in membrane protein crystallization. J. Appl. Cryst. 38, 398-400 (2005).
    • (2005) J. Appl. Cryst , vol.38 , pp. 398-400
    • Cherezov, V.1    Caffrey, M.2
  • 31
    • 0033932850 scopus 로고    scopus 로고
    • Membrane protein crystallization in lipidic mesophases: Detergent effect
    • Ai, X. & Caffrey, M. Membrane protein crystallization in lipidic mesophases: detergent effect. Biophys. J. 79, 394-405 (2000).
    • (2000) Biophys. J , vol.79 , pp. 394-405
    • Ai, X.1    Caffrey, M.2
  • 32
    • 0242385349 scopus 로고    scopus 로고
    • Detergents destabilize the cubic phase of monoolein: Implications for membrane protein crystallization
    • Misquitta, Y. & Caffrey, M. Detergents destabilize the cubic phase of monoolein: implications for membrane protein crystallization. Biophys. J. 85, 3084-3096 (2003).
    • (2003) Biophys. J , vol.85 , pp. 3084-3096
    • Misquitta, Y.1    Caffrey, M.2
  • 33
    • 0032422462 scopus 로고    scopus 로고
    • Simple mechanical mixer for small viscous lipid-containing samples
    • Cheng, A., Hummel, B., Qiu, H. & Caffrey, M. A simple mechanical mixer for small viscous lipid-containing samples. Chem. Phys. Lipids 95, 11-21 (1998).
    • (1998) Chem. Phys. Lipids , vol.95 , pp. 11-21
    • Cheng, A.1    Hummel, B.2    Qiu, H.3    Caffrey, M.A.4
  • 35
    • 5144234232 scopus 로고    scopus 로고
    • Rational design of lipid for membrane protein crystallization
    • Misquitta, Y. et al. Rational design of lipid for membrane protein crystallization. J. Struct. Biol. 148, 169-175 (2004).
    • (2004) J. Struct. Biol , vol.148 , pp. 169-175
    • Misquitta, Y.1
  • 36
    • 29144462483 scopus 로고    scopus 로고
    • UV microscopy at 280 nm is effective in screening forthe growth of protein microcrystals
    • Lunde, C.S. et al. UV microscopy at 280 nm is effective in screening forthe growth of protein microcrystals. J. Appl. Cryst. 38, 1031-1034 (2005).
    • (2005) J. Appl. Cryst , vol.38 , pp. 1031-1034
    • Lunde, C.S.1
  • 37
    • 0030565904 scopus 로고    scopus 로고
    • The crystallization of biological macromolecules from precipitates: Evidence for Ostwald ripening
    • Ng, J.D. et al. The crystallization of biological macromolecules from precipitates: evidence for Ostwald ripening. J. Cryst. Growth 168, 50-62 (1996).
    • (1996) J. Cryst. Growth , vol.168 , pp. 50-62
    • Ng, J.D.1
  • 38
    • 34548558727 scopus 로고    scopus 로고
    • Crystallization ofsoluble proteinsin vapordiffusion for x-ray crystallography. Nat
    • Benvenuti, M. & Mangani, S. Crystallization ofsoluble proteinsin vapordiffusion for x-ray crystallography. Nat. Protoc. 2,1633-1651 (2007).
    • (2007) Protoc , vol.2 , pp. 1633-1651
    • Benvenuti, M.1    Mangani, S.2
  • 39
    • 0032414367 scopus 로고    scopus 로고
    • Enzymic release of crystals from lipidic cubic phases. Biochem. Soc
    • Nollert, P. & Landau, E.M. Enzymic release of crystals from lipidic cubic phases. Biochem. Soc. Trans. 26, 709-713 (1998).
    • (1998) Trans , vol.26 , pp. 709-713
    • Nollert, P.1    Landau, E.M.2
  • 41
    • 4344625042 scopus 로고    scopus 로고
    • Macromolecular cryocrystallography—methods for cooling and mounting protein crystals at cryogenic temperatures
    • Pflugrath, J.W. Macromolecular cryocrystallography—methods for cooling and mounting protein crystals at cryogenic temperatures. Methods 34, 415-423 (2004).
    • (2004) Methods , vol.34 , pp. 415-423
    • Pflugrath, J.W.1
  • 42
    • 15444380710 scopus 로고    scopus 로고
    • Gramicidin structure and disposition in highly curved membranes
    • Liu, W. & Caffrey, M. Gramicidin structure and disposition in highly curved membranes. J. Struct. Biol. 150, 23-40 (2005).
    • (2005) J. Struct. Biol , vol.150 , pp. 23-40
    • Liu, W.1    Caffrey, M.2
  • 43
    • 0032553533 scopus 로고    scopus 로고
    • Purification and characterization of monomeric Escherichia coli vitamin B12 receptor with high affinity for colicin E3
    • Taylor, R., Burgner, J.W., Clifton, J. & Cramer, W.A. Purification and characterization of monomeric Escherichia coli vitamin B12 receptor with high affinity for colicin E3. J. Biol. Chem. 273, 31113-31118 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 31113-31118
    • Taylor, R.1    Burgner, J.W.2    Clifton, J.3    Cramer, W.A.4
  • 44
    • 0024358023 scopus 로고
    • Crystallization and characterization of two crystal forms of the B800-850 light-harvesting complex from Rhodopseudomonas acidophila strain 10050
    • Papiz, M.Z. et al. Crystallization and characterization of two crystal forms of the B800-850 light-harvesting complex from Rhodopseudomonas acidophila strain 10050. J. Mol. Biol. 209, 833-835 (1989).
    • (1989) J. Mol. Biol , vol.209 , pp. 833-835
    • Papiz, M.Z.1
  • 45
    • 0034909320 scopus 로고    scopus 로고
    • Expression, refolding and crystallization of the OpcA invasin from Neisseria meningitidis
    • Prince, S.M. et al. Expression, refolding and crystallization of the OpcA invasin from Neisseria meningitidis. Acta Crystallogr. D Biol. Crystallogr. 57, 1164-1166 (2001).
    • (2001) Acta Crystallogr. D Biol. Crystallogr , vol.57 , pp. 1164-1166
    • Prince, S.M.1
  • 46
    • 36448978229 scopus 로고    scopus 로고
    • GPCR engineering yields high-resolution structural insights into beta2-adrenergic receptor function
    • Rosenbaum, D.M. et al. GPCR engineering yields high-resolution structural insights into beta2-adrenergic receptor function. Science 318, 1266-1273 (2007).
    • (2007) Science , vol.318 , pp. 1266-1273
    • Rosenbaum, D.M.1
  • 47
    • 34547803687 scopus 로고    scopus 로고
    • Membrane protein crystallization in lipidic mesophases. A mechanism study using X-ray microdiffraction
    • Cherezov, V. & Caffrey, M. Membrane protein crystallization in lipidic mesophases. A mechanism study using X-ray microdiffraction. Faraday Discuss. 136, 195-212 (2007).
    • (2007) Faraday Discuss , vol.136 , pp. 195-212
    • Cherezov, V.1    Caffrey, M.2
  • 48
    • 0034961077 scopus 로고    scopus 로고
    • Crystallization screens: Compatibility with the lipidic cubic phase for in meso crystallization of membrane proteins
    • Cherezov, V., Fersi, H. & Caffrey, M. Crystallization screens: compatibility with the lipidic cubic phase for in meso crystallization of membrane proteins. Biophys. J. 81, 225-242 (2001).
    • (2001) Biophys. J , vol.81 , pp. 225-242
    • Cherezov, V.1    Fersi, H.2    Caffrey, M.3
  • 49
    • 0023646686 scopus 로고
    • Kinetics and mechanism of transitions involving the lamellar, cubic, inverted hexagonal, and fluid isotropic phases of hydrated monoacylglycerides monitored by time-resolved X-ray diffraction
    • Caffrey, M. Kinetics and mechanism of transitions involving the lamellar, cubic, inverted hexagonal, and fluid isotropic phases of hydrated monoacylglycerides monitored by time-resolved X-ray diffraction. Biochemistry 26, 6349-6363 (1987).
    • (1987) Biochemistry , vol.26 , pp. 6349-6363
    • Caffrey, M.1
  • 50
    • 0036106309 scopus 로고    scopus 로고
    • Biophysical and transfection studies of the diC(14)-amidine/ DNA complex
    • Cherezov, V. et al. Biophysical and transfection studies of the diC(14)-amidine/ DNA complex. Biophys. J. 82, 3105-3117 (2002).
    • (2002) Biophys. J , vol.82 , pp. 3105-3117
    • Cherezov, V.1
  • 51
    • 84971942068 scopus 로고
    • JCPDS—International Centre for Diffraction Data round robin study of silver behenate. A possible low-angle X-ray diffraction calibration standard
    • Blanton, T.N. et al. JCPDS—International Centre for Diffraction Data round robin study of silver behenate. A possible low-angle X-ray diffraction calibration standard. Powder Diffr. 10, 91-95 (1995).
    • (1995) Powder Diffr , vol.10 , pp. 91-95
    • Blanton, T.N.1
  • 52
    • 0027181230 scopus 로고
    • Thermodynamic, thermomechanical, and structural properties of a hydrated asymmetric phosphatidylcholine
    • Zhu, T. & Caffrey, M. Thermodynamic, thermomechanical, and structural properties of a hydrated asymmetric phosphatidylcholine. Biophys. J. 65, 939-954 (1993).
    • (1993) Biophys. J , vol.65 , pp. 939-954
    • Zhu, T.1    Caffrey, M.2
  • 53
    • 0036848784 scopus 로고    scopus 로고
    • Too hot to handle? Synchrotron X-ray damage of lipid membranes and mesophases
    • Cherezov, V., Riedl, K.M. & Caffrey, M. Too hot to handle? Synchrotron X-ray damage of lipid membranes and mesophases. J. Synchrotron Radiat. 9, 333-341 (2002).
    • (2002) J. Synchrotron Radiat , vol.9 , pp. 333-341
    • Cherezov, V.1    Riedl, K.M.2    Caffrey, M.3
  • 55
    • 0019891830 scopus 로고
    • Fluorescence quenching in model membranes. 3. Relationship between calcium adenosinetriphosphatase enzyme activity and the affinity of the protein for phosphatidylcholines with different acyl chain characteristics
    • Caffrey, M. & Feigenson, G.W. Fluorescence quenching in model membranes. 3. Relationship between calcium adenosinetriphosphatase enzyme activity and the affinity of the protein for phosphatidylcholines with different acyl chain characteristics. Biochemistry 20, 1949-1961 (1981).
    • (1981) Biochemistry , vol.20 , pp. 1949-1961
    • Caffrey, M.1    Feigenson, G.W.2
  • 56
    • 9944220520 scopus 로고    scopus 로고
    • Membrane protein crystallization in lipidic mesophases with tailored bilayers
    • Misquitta, L.V. et al. Membrane protein crystallization in lipidic mesophases with tailored bilayers. Structure 12, 2113-2124 (2004).
    • (2004) Structure , vol.12 , pp. 2113-2124
    • Misquitta, L.V.1
  • 57
    • 0036929858 scopus 로고    scopus 로고
    • Membrane protein crystallization in meso: Lipid type-tailoring ofthe cubic phase
    • Cherezov, V., Clogston, J., Misquitta, Y., Abdel-Gawad, W. & Caffrey, M. Membrane protein crystallization in meso: lipid type-tailoring ofthe cubic phase. Biophys. J. 83, 3393-3407 (2002).
    • (2002) Biophys. J , vol.83 , pp. 3393-3407
    • Cherezov, V.1    Clogston, J.2    Misquitta, Y.3    Abdel-Gawad, W.4    Caffrey, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.