메뉴 건너뛰기




Volumn 1751, Issue 2, 2005, Pages 213-216

Crystallization of bacteriorhodopsin solubilized by a tripod amphiphile

Author keywords

Bacteriorhodopsin; Crystallization; Detergent; Membrane protein; Surfactant; Tripod amphiphile

Indexed keywords

AMPHOPHILE; BACTERIORHODOPSIN; MEMBRANE PROTEIN; MONOMER; SURFACTANT;

EID: 23444454016     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.04.011     Document Type: Article
Times cited : (16)

References (29)
  • 1
    • 0037333304 scopus 로고    scopus 로고
    • Membrane proteins: The 'Wild West' of structural biology
    • J. Torres, T.J. Stevens, and M. Samson Membrane proteins: the 'Wild West' of structural biology Trends Biochem. Sci. 28 2003 137 144
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 137-144
    • Torres, J.1    Stevens, T.J.2    Samson, M.3
  • 2
    • 0037391107 scopus 로고    scopus 로고
    • Membrane protein crystallization
    • M. Caffrey Membrane protein crystallization J. Struct. Biol. 142 2003 108 132
    • (2003) J. Struct. Biol. , vol.142 , pp. 108-132
    • Caffrey, M.1
  • 5
    • 0024117785 scopus 로고
    • Three-dimensional crystallization of membrane proteins
    • W. Kühlbrandt Three-dimensional crystallization of membrane proteins Q. Rev. Biophys. 21 1988 429 477
    • (1988) Q. Rev. Biophys. , vol.21 , pp. 429-477
    • Kühlbrandt, W.1
  • 6
    • 0016657917 scopus 로고
    • Solubilization of membrane proteins by detergents
    • A. Helenius, and K. Simons Solubilization of membrane proteins by detergents Biochim. Biophys. Acta 415 1975 29 79
    • (1975) Biochim. Biophys. Acta , vol.415 , pp. 29-79
    • Helenius, A.1    Simons, K.2
  • 8
    • 0035980050 scopus 로고    scopus 로고
    • Detergents as tools in membrane biochemistry
    • R.M. Garavito, and S. Ferguson-Miller Detergents as tools in membrane biochemistry J. Biol. Chem. 276 2001 32403 32406
    • (2001) J. Biol. Chem. , vol.276 , pp. 32403-32406
    • Garavito, R.M.1    Ferguson-Miller, S.2
  • 9
    • 0242663865 scopus 로고    scopus 로고
    • Separation methods in the analysis of protein membrane complexes
    • Y. Kashino Separation methods in the analysis of protein membrane complexes J. Chromatogr., B, Biomed. Sci. Appl. 797 2003 191 216
    • (2003) J. Chromatogr., B, Biomed. Sci. Appl. , vol.797 , pp. 191-216
    • Kashino, Y.1
  • 10
    • 0030451437 scopus 로고    scopus 로고
    • Amphipols: Polymers that keep membrane proteins soluble in aqueous solutions
    • C. Tribet, R. Audebert, and J.L. Popot Amphipols: polymers that keep membrane proteins soluble in aqueous solutions Proc. Natl. Acad. Sci. U. S. A. 93 1996 15047 15050
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 15047-15050
    • Tribet, C.1    Audebert, R.2    Popot, J.L.3
  • 11
    • 0034425014 scopus 로고    scopus 로고
    • Nonionic amphiphilic polymers derived from Tris(hydroxymethyl)- acrylamidomethane keep membrane proteins soluble and native in the absence of detergent
    • C. Prata, F. Giusti, Y. Gohon, B. Pucci, J.L. Popot, and C. Tribet Nonionic amphiphilic polymers derived from Tris(hydroxymethyl)-acrylamidomethane keep membrane proteins soluble and native in the absence of detergent Biopolymers 56 2000 77 84
    • (2000) Biopolymers , vol.56 , pp. 77-84
    • Prata, C.1    Giusti, F.2    Gohon, Y.3    Pucci, B.4    Popot, J.L.5    Tribet, C.6
  • 16
    • 0034822665 scopus 로고    scopus 로고
    • Existing and emergent roles for surfactants in the three-dimensional crystallization of integral membrane proteins
    • M.C. Wiener Existing and emergent roles for surfactants in the three-dimensional crystallization of integral membrane proteins Curr. Opin. Colloid Interface Sci. 6 2001 412 419
    • (2001) Curr. Opin. Colloid Interface Sci. , vol.6 , pp. 412-419
    • Wiener, M.C.1
  • 17
    • 0002467417 scopus 로고
    • Detergent phenomena in membrane protein crystallization
    • H. Michel CRC Press, Inc. Boca Raton
    • M. Zulauf Detergent phenomena in membrane protein crystallization H. Michel Crystallization of Membrane Proteins 1991 CRC Press, Inc. Boca Raton 54 71
    • (1991) Crystallization of Membrane Proteins , pp. 54-71
    • Zulauf, M.1
  • 18
    • 0025643463 scopus 로고
    • The critical role of detergents in the crystallization of membrane proteins
    • J.P. Rosenbusch The critical role of detergents in the crystallization of membrane proteins J. Struct. Biol. 104 1990 134 138
    • (1990) J. Struct. Biol. , vol.104 , pp. 134-138
    • Rosenbusch, J.P.1
  • 19
    • 0035239215 scopus 로고    scopus 로고
    • Approaches to determining membrane protein structures to high resolution: Do selections of subpopulations occur?
    • J.P. Rosenbusch, A. Lustig, M. Grabo, M. Zulauf, and M. Regenass Approaches to determining membrane protein structures to high resolution: do selections of subpopulations occur? Micron 32 2001 75 90
    • (2001) Micron , vol.32 , pp. 75-90
    • Rosenbusch, J.P.1    Lustig, A.2    Grabo, M.3    Zulauf, M.4    Regenass, M.5
  • 21
    • 0029992660 scopus 로고    scopus 로고
    • Lipidic cubic phases: A novel concept for the crystallization of membrane proteins
    • E.M. Landau, and J.P. Rosenbusch Lipidic cubic phases: a novel concept for the crystallization of membrane proteins Proc. Natl. Acad. Sci. U. S. A. 93 1996 14532 14535
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 14532-14535
    • Landau, E.M.1    Rosenbusch, J.P.2
  • 22
    • 0036301007 scopus 로고    scopus 로고
    • Bicelle crystallization: A new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure
    • S. Faham, and J.U. Bowie Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure J. Mol. Biol. 316 2002 1 6
    • (2002) J. Mol. Biol. , vol.316 , pp. 1-6
    • Faham, S.1    Bowie, J.U.2
  • 23
    • 0032561127 scopus 로고    scopus 로고
    • A novel three-dimensional crystal of bacteriorhodopsin obtained by successive fusion of the vesicular assemblies
    • K. Takeda, H. Sato, T. Hino, M. Kono, K. Fukuda, I. Sakurai, T. Okada, and T. Kouyama A novel three-dimensional crystal of bacteriorhodopsin obtained by successive fusion of the vesicular assemblies J. Mol. Biol. 283 1998 463 474
    • (1998) J. Mol. Biol. , vol.283 , pp. 463-474
    • Takeda, K.1    Sato, H.2    Hino, T.3    Kono, M.4    Fukuda, K.5    Sakurai, I.6    Okada, T.7    Kouyama, T.8
  • 24
    • 0000095071 scopus 로고
    • Three-dimensional crystals of membrane proteins: Bacteriorhodopsin
    • H. Michel, and D. Oesterhelt Three-dimensional crystals of membrane proteins: bacteriorhodopsin Proc. Natl. Acad. Sci. U. S. A. 77 1980 1283 1285
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 1283-1285
    • Michel, H.1    Oesterhelt, D.2
  • 25
    • 0027504943 scopus 로고
    • Orthorhombic crystal form of bacteriorhodopsin nucleated on benzamidine diffracting to 3.6 Å resolution
    • G.F. Schertler, H.D. Bartunik, H. Michel, and D. Oesterhelt Orthorhombic crystal form of bacteriorhodopsin nucleated on benzamidine diffracting to 3.6 Å resolution J. Mol. Biol. 234 1993 156 164
    • (1993) J. Mol. Biol. , vol.234 , pp. 156-164
    • Schertler, G.F.1    Bartunik, H.D.2    Michel, H.3    Oesterhelt, D.4
  • 26
    • 0032578378 scopus 로고    scopus 로고
    • Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex
    • L. Essen, R. Siegert, W.D. Lehmann, and D. Oesterhelt Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex Proc. Natl. Acad. Sci. U. S. A. 95 1998 11673 11678
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 11673-11678
    • Essen, L.1    Siegert, R.2    Lehmann, W.D.3    Oesterhelt, D.4
  • 28
    • 0013673916 scopus 로고
    • Isolation of purple membranes
    • F.T. Robb A.R. Place K.R. Sowers H.J. Schreier S. DasSarma E.M. Fleischmann Cold Spring Harbor Laboratory Press Cold Spring Harbor
    • D. Oesterhelt Isolation of purple membranes F.T. Robb A.R. Place K.R. Sowers H.J. Schreier S. DasSarma E.M. Fleischmann Archaea: A Laboratory Manual 1995 Cold Spring Harbor Laboratory Press Cold Spring Harbor 55 58
    • (1995) Archaea: A Laboratory Manual , pp. 55-58
    • Oesterhelt, D.1
  • 29
    • 33644563595 scopus 로고    scopus 로고
    • J.U. Bowie, www.doe-mbi.ucla.edu/∼salem/bicelle_method_faq.html. 2004.
    • (2004)
    • Bowie, J.U.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.