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Volumn 1610, Issue 1, 2003, Pages 37-45

The expression of outer membrane proteins for crystallization

Author keywords

Detergent extraction; Detergent micelle; Eukaryotic organellar outer membrane; Functional expression; In vitro (re)folding; Inclusion body

Indexed keywords

DETERGENT; OUTER MEMBRANE PROTEIN;

EID: 0037450548     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(02)00711-3     Document Type: Review
Times cited : (67)

References (95)
  • 1
    • 0027640084 scopus 로고
    • Bacterial porins: Structure and function
    • Schulz G.E. Bacterial porins: structure and function. Curr. Opin. Cell Biol. 5:1993;701-707.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 701-707
    • Schulz, G.E.1
  • 2
    • 0037064291 scopus 로고    scopus 로고
    • The structure of bacterial outer membrane proteins
    • Schulz G.E. The structure of bacterial outer membrane proteins. Biochim. Biophys. Acta. 1565:2002;308-317.
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 308-317
    • Schulz, G.E.1
  • 4
    • 0030220261 scopus 로고    scopus 로고
    • Porins: General to specific, native to engineered passive pores
    • Schulz G.E. Porins: general to specific, native to engineered passive pores. Curr. Opin. Struct. Biol. 6:1996;485-490.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 485-490
    • Schulz, G.E.1
  • 6
    • 0036902040 scopus 로고    scopus 로고
    • OmpA membrane domain as a tight-binding anchor for lipid bilayers
    • Ringler P., Schulz G.E. OmpA membrane domain as a tight-binding anchor for lipid bilayers. Chem. Bio. Chem. 3:2002;463-466.
    • (2002) Chem. Bio. Chem. , vol.3 , pp. 463-466
    • Ringler, P.1    Schulz, G.E.2
  • 7
    • 0037412185 scopus 로고    scopus 로고
    • Asymmetric conductivity of engineered porins
    • Bannwarth M., Schulz G.E. Asymmetric conductivity of engineered porins. Protein Eng. 15:2002;799-804.
    • (2002) Protein Eng. , vol.15 , pp. 799-804
    • Bannwarth, M.1    Schulz, G.E.2
  • 8
    • 0019036909 scopus 로고
    • Three-dimensional crystals of an integral membrane protein: An initial X-ray analysis
    • Garavito R.M., Rosenbusch J.P. Three-dimensional crystals of an integral membrane protein: an initial X-ray analysis. J. Cell Biol. 86:1980;327-329.
    • (1980) J. Cell Biol. , vol.86 , pp. 327-329
    • Garavito, R.M.1    Rosenbusch, J.P.2
  • 9
    • 0024571246 scopus 로고
    • Crystallization and preliminary X-ray analysis of porin from Rhodobacter capsulatus
    • Nestel U., Wacker T., Woitzik D., Weckesser J., Kreutz W., Welte W. Crystallization and preliminary X-ray analysis of porin from Rhodobacter capsulatus. FEBS Lett. 242:1989;405-408.
    • (1989) FEBS Lett. , vol.242 , pp. 405-408
    • Nestel, U.1    Wacker, T.2    Woitzik, D.3    Weckesser, J.4    Kreutz, W.5    Welte, W.6
  • 11
    • 0025345316 scopus 로고
    • The three-dimensional structure of porin from Rhodobacter capsulatus at 3 Å resolution
    • Weiss M.S., Wacker T., Weckesser J., Welte W., Schulz G.E. The three-dimensional structure of porin from Rhodobacter capsulatus at 3 Å resolution. FEBS Lett. 267:1990;268-272.
    • (1990) FEBS Lett. , vol.267 , pp. 268-272
    • Weiss, M.S.1    Wacker, T.2    Weckesser, J.3    Welte, W.4    Schulz, G.E.5
  • 12
    • 0026079026 scopus 로고
    • Crystals of an integral membrane protein diffracting to 1.8 Å resolution
    • Kreusch A., Weiss M.S., Welte W., Weckesser J., Schulz G.E. Crystals of an integral membrane protein diffracting to 1.8 Å resolution. J. Mol. Biol. 217:1991;9-10.
    • (1991) J. Mol. Biol. , vol.217 , pp. 9-10
    • Kreusch, A.1    Weiss, M.S.2    Welte, W.3    Weckesser, J.4    Schulz, G.E.5
  • 14
    • 0026331041 scopus 로고
    • Molecular architecture and electrostatic properties of a bacterial porin
    • Weiss M.S., Abele U., Weckesser J., Welte W., Schiltz E., Schulz G.E. Molecular architecture and electrostatic properties of a bacterial porin. Science. 254:1991;1627-1630.
    • (1991) Science , vol.254 , pp. 1627-1630
    • Weiss, M.S.1    Abele, U.2    Weckesser, J.3    Welte, W.4    Schiltz, E.5    Schulz, G.E.6
  • 16
    • 0026737314 scopus 로고
    • Structure of porin refined at 1.8 Å resolution
    • Weiss M.S., Schulz G.E. Structure of porin refined at 1.8 Å resolution. J. Mol. Biol. 227:1992;493-509.
    • (1992) J. Mol. Biol. , vol.227 , pp. 493-509
    • Weiss, M.S.1    Schulz, G.E.2
  • 17
    • 0028140564 scopus 로고
    • The structure of the membrane channel porin from Rhodopseudomonas blastica at 2.0 Å resolution
    • Kreusch A., Neubüser A., Schiltz E., Weckesser J., Schulz G.E. The structure of the membrane channel porin from Rhodopseudomonas blastica at 2.0 Å resolution. Protein Sci. 3:1994;58-63.
    • (1994) Protein Sci. , vol.3 , pp. 58-63
    • Kreusch, A.1    Neubüser, A.2    Schiltz, E.3    Weckesser, J.4    Schulz, G.E.5
  • 18
    • 0031557404 scopus 로고    scopus 로고
    • Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside
    • Meyer J.E.W., Hofnung M., Schulz G.E. Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside. J. Mol. Biol. 266:1997;761-775.
    • (1997) J. Mol. Biol. , vol.266 , pp. 761-775
    • Meyer, J.E.W.1    Hofnung, M.2    Schulz, G.E.3
  • 19
    • 0030902082 scopus 로고    scopus 로고
    • Energy profile of maltooligosaccharide permeation through maltoporin as derived from the structure and from a statistical analysis of saccharide-protein interactions
    • Meyer J.E.W., Schulz G.E. Energy profile of maltooligosaccharide permeation through maltoporin as derived from the structure and from a statistical analysis of saccharide-protein interactions. Protein Sci. 6:1997;1084-1091.
    • (1997) Protein Sci. , vol.6 , pp. 1084-1091
    • Meyer, J.E.W.1    Schulz, G.E.2
  • 21
    • 0025138218 scopus 로고
    • Crystallization and preliminary X-ray characterization of maltoporin from Escherichia coli
    • Stauffer K.A., Page M.G.P., Hardmeyer A., Keller T.A., Pauptit R.A. Crystallization and preliminary X-ray characterization of maltoporin from Escherichia coli. J. Mol. Biol. 211:1989;297-299.
    • (1989) J. Mol. Biol. , vol.211 , pp. 297-299
    • Stauffer, K.A.1    Page, M.G.P.2    Hardmeyer, A.3    Keller, T.A.4    Pauptit, R.A.5
  • 22
    • 0027471832 scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of ScrY, a specific bacterial outer membrane porin
    • Forst D., Schülein K., Wacker T., Diederichs K., Kreutz W., Benz R., Welte W. Crystallization and preliminary X-ray diffraction analysis of ScrY, a specific bacterial outer membrane porin. J. Mol. Biol. 229:1993;258-262.
    • (1993) J. Mol. Biol. , vol.229 , pp. 258-262
    • Forst, D.1    Schülein, K.2    Wacker, T.3    Diederichs, K.4    Kreutz, W.5    Benz, R.6    Welte, W.7
  • 23
    • 0031822853 scopus 로고    scopus 로고
    • An internal affinity-tag for purification and crystallization of the siderophore receptor FhuA, integral outer membrane protein from Escherichia coli K-12
    • Ferguson A.D., Breed J., Diederichs K., Welte W., Coulton J.W. An internal affinity-tag for purification and crystallization of the siderophore receptor FhuA, integral outer membrane protein from Escherichia coli K-12. Protein Sci. 7:1998;1636-1638.
    • (1998) Protein Sci. , vol.7 , pp. 1636-1638
    • Ferguson, A.D.1    Breed, J.2    Diederichs, K.3    Welte, W.4    Coulton, J.W.5
  • 24
    • 0033373495 scopus 로고    scopus 로고
    • Overexpression and refolding of an 80-kDa iron transporter from the outer membrane of Escherichia coli
    • Buchanan S.K. Overexpression and refolding of an 80-kDa iron transporter from the outer membrane of Escherichia coli. Biochem. Soc. Trans. 27:1999;903-908.
    • (1999) Biochem. Soc. Trans. , vol.27 , pp. 903-908
    • Buchanan, S.K.1
  • 26
    • 0031014882 scopus 로고    scopus 로고
    • Structure of TolC, the outer membrane component of the bacterial type I efflux system, derived from two-dimensional crystals
    • Koronakis V., Li J., Koronakis E., Stauffer K. Structure of TolC, the outer membrane component of the bacterial type I efflux system, derived from two-dimensional crystals. Mol. Microbiol. 23:1997;617-623.
    • (1997) Mol. Microbiol. , vol.23 , pp. 617-623
    • Koronakis, V.1    Li, J.2    Koronakis, E.3    Stauffer, K.4
  • 27
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • Koronakis V., Sharff A., Koronakis E., Luisi B., Hughes C. Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature. 405:2000;914-919.
    • (2000) Nature , vol.405 , pp. 914-919
    • Koronakis, V.1    Sharff, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 28
    • 0035099425 scopus 로고    scopus 로고
    • Strategies for prokaryotic expression of eukaryotic membrane proteins
    • Laage R., Langosch D. Strategies for prokaryotic expression of eukaryotic membrane proteins. Traffic. 2:2001;99-104.
    • (2001) Traffic , vol.2 , pp. 99-104
    • Laage, R.1    Langosch, D.2
  • 29
    • 18744422713 scopus 로고    scopus 로고
    • Expression of porin from Rhodopseudomonas blastica in Escherichia coli inclusion bodies and folding into exact native structure
    • Schmid B., Krömer M., Schulz G.E. Expression of porin from Rhodopseudomonas blastica in Escherichia coli inclusion bodies and folding into exact native structure. FEBS Lett. 381:1996;111-114.
    • (1996) FEBS Lett. , vol.381 , pp. 111-114
    • Schmid, B.1    Krömer, M.2    Schulz, G.E.3
  • 30
    • 0032127999 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of ferric enterobactin receptor FepA, an integral membrane protein from Escherichia coli
    • Smith B.S., Kobe B., Kurumbail R., Buchanan S.K., Venkatramoni L., van der Helm D., Deisenhofer J. Crystallization and preliminary X-ray analysis of ferric enterobactin receptor FepA, an integral membrane protein from Escherichia coli. Acta Crystallogr., D. 54:1998;697-699.
    • (1998) Acta Crystallogr., D , vol.54 , pp. 697-699
    • Smith, B.S.1    Kobe, B.2    Kurumbail, R.3    Buchanan, S.K.4    Venkatramoni, L.5    Van der Helm, D.6    Deisenhofer, J.7
  • 31
    • 0030850807 scopus 로고    scopus 로고
    • Oligomeric states and siderophore binding of the ligand-gated FhuA protein that forms channels across Escherichia coli outer membranes
    • Locher K.P., Rosenbusch J.P. Oligomeric states and siderophore binding of the ligand-gated FhuA protein that forms channels across Escherichia coli outer membranes. Eur. J. Biochem. 247:1997;770-775.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 770-775
    • Locher, K.P.1    Rosenbusch, J.P.2
  • 32
    • 0034816414 scopus 로고    scopus 로고
    • Overexpression, refolding, and purification of the histidine-tagged outer membrane efflux protein OprM of Pseudomonas aeruginosa
    • Charbonnier F., Köhler T., Pechère J.C., Ducruix A. Overexpression, refolding, and purification of the histidine-tagged outer membrane efflux protein OprM of Pseudomonas aeruginosa. Protein Expr. Purif. 23:2001;121-127.
    • (2001) Protein Expr. Purif. , vol.23 , pp. 121-127
    • Charbonnier, F.1    Köhler, T.2    Pechère, J.C.3    Ducruix, A.4
  • 33
    • 0029101182 scopus 로고
    • In vitro folding of Escherichia coli outer-membrane phospholipase A
    • Dekker N., Merck K., Tommassen J., Verheij H.M. In vitro folding of Escherichia coli outer-membrane phospholipase A. Eur. J. Biochem. 232:1995;214-219.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 214-219
    • Dekker, N.1    Merck, K.2    Tommassen, J.3    Verheij, H.M.4
  • 34
    • 0028980657 scopus 로고
    • Crystallization and preliminary X-ray analysis of outer membrane phospholipase A from Escherichia coli
    • Blaauw M., Dekker N., Verheij H.M., Kalk K.H., Dijkstra B.W. Crystallization and preliminary X-ray analysis of outer membrane phospholipase A from Escherichia coli. FEBS Lett. 373:1995;10-12.
    • (1995) FEBS Lett. , vol.373 , pp. 10-12
    • Blaauw, M.1    Dekker, N.2    Verheij, H.M.3    Kalk, K.H.4    Dijkstra, B.W.5
  • 36
    • 0000983237 scopus 로고    scopus 로고
    • In vitro folding, purification and characterization of Escherichia coli outer membrane protease OmpT
    • Kramer R.A., Zandwijken D., Egmond M.R., Dekker N. In vitro folding, purification and characterization of Escherichia coli outer membrane protease OmpT. Eur. J. Biochem. 267:2000;885-893.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 885-893
    • Kramer, R.A.1    Zandwijken, D.2    Egmond, M.R.3    Dekker, N.4
  • 38
    • 0035903650 scopus 로고    scopus 로고
    • Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site
    • Vandeputte-Rutten L., Kramer R.A., Kroon J., Dekker N., Egmond M.R., Gros P. Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site. EMBO J. 20:2001;5033-5039.
    • (2001) EMBO J. , vol.20 , pp. 5033-5039
    • Vandeputte-Rutten, L.1    Kramer, R.A.2    Kroon, J.3    Dekker, N.4    Egmond, M.R.5    Gros, P.6
  • 39
    • 0033784649 scopus 로고    scopus 로고
    • Expression, two-dimensional crystallization, and three-dimensional reconstruction of the β8 outer membrane protein Omp21 from Comamonas acidovorans
    • Baldermann C., Engelhardt H. Expression, two-dimensional crystallization, and three-dimensional reconstruction of the β8 outer membrane protein Omp21 from Comamonas acidovorans. J. Struct. Biol. 131:2000;96-107.
    • (2000) J. Struct. Biol. , vol.131 , pp. 96-107
    • Baldermann, C.1    Engelhardt, H.2
  • 40
    • 0032584765 scopus 로고    scopus 로고
    • Refolding of Escherichia coli produced membrane protein inclusion bodies immobilized by nickel chelating chromatography
    • Rogl H., Kosemund K., Kühlbrandt W., Collinson I. Refolding of Escherichia coli produced membrane protein inclusion bodies immobilized by nickel chelating chromatography. FEBS Lett. 432:1998;21-26.
    • (1998) FEBS Lett. , vol.432 , pp. 21-26
    • Rogl, H.1    Kosemund, K.2    Kühlbrandt, W.3    Collinson, I.4
  • 42
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • Studier F.W. Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. J. Mol. Biol. 219:1991;37-44.
    • (1991) J. Mol. Biol. , vol.219 , pp. 37-44
    • Studier, F.W.1
  • 43
    • 0033932639 scopus 로고    scopus 로고
    • Beta-barrel membrane proteins
    • Schulz G.E. Beta-barrel membrane proteins. Curr. Opin. Struct. Biol. 10:2000;443-447.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 443-447
    • Schulz, G.E.1
  • 44
    • 0031448082 scopus 로고    scopus 로고
    • On the structure and gating mechanism of the mitochondrial channel, VDAC
    • Mannella C.A. On the structure and gating mechanism of the mitochondrial channel, VDAC. J. Bioenerg. Biomembranes. 29:1997;525-531.
    • (1997) J. Bioenerg. Biomembranes , vol.29 , pp. 525-531
    • Mannella, C.A.1
  • 45
    • 0031857554 scopus 로고    scopus 로고
    • Conformational changes in the mitochondrial channel protein, VDAC, and their functional implications
    • Mannella C.A. Conformational changes in the mitochondrial channel protein, VDAC, and their functional implications. J. Struct. Biol. 121:1998;207-218.
    • (1998) J. Struct. Biol. , vol.121 , pp. 207-218
    • Mannella, C.A.1
  • 46
    • 0036140732 scopus 로고    scopus 로고
    • Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders
    • Binda C., Newton-Vinson P., Hubalek F., Edmondson D.E., Mattevi A. Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders. Nat. Struct. Biol. 9:2002;22-26.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 22-26
    • Binda, C.1    Newton-Vinson, P.2    Hubalek, F.3    Edmondson, D.E.4    Mattevi, A.5
  • 47
    • 0034641678 scopus 로고    scopus 로고
    • In vitro reconstitution and biophysical characterization of OEP16, an outer envelope pore protein of pea chloroplasts
    • Linke D., Frank J., Holzwarth J.F., Soll J., Boettcher C., Fromme P. In vitro reconstitution and biophysical characterization of OEP16, an outer envelope pore protein of pea chloroplasts. Biochemistry. 39:2000;11050-11056.
    • (2000) Biochemistry , vol.39 , pp. 11050-11056
    • Linke, D.1    Frank, J.2    Holzwarth, J.F.3    Soll, J.4    Boettcher, C.5    Fromme, P.6
  • 48
    • 0033178531 scopus 로고    scopus 로고
    • β-Barrel proteins from bacterial outer membranes: Structure, function and refolding
    • Buchanan S.K. β-Barrel proteins from bacterial outer membranes: structure, function and refolding. Curr. Opin. Struct. Biol. 9:1999;455-461.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 455-461
    • Buchanan, S.K.1
  • 49
    • 0033773601 scopus 로고    scopus 로고
    • High-level expression of human liver monoamine oxidase B in Pichia pastoris
    • Newton-Vinson P., Hubalek F., Edmondson D.E. High-level expression of human liver monoamine oxidase B in Pichia pastoris. Protein Expr. Purif. 20:2000;334-345.
    • (2000) Protein Expr. Purif. , vol.20 , pp. 334-345
    • Newton-Vinson, P.1    Hubalek, F.2    Edmondson, D.E.3
  • 50
    • 0032875663 scopus 로고    scopus 로고
    • Crystallization of the human, mitochondrial voltage-dependent anion-selective channel in the presence of phospholipids
    • Dolder M., Zeth K., Tittmann P., Gross H., Welte W., Wallimann T. Crystallization of the human, mitochondrial voltage-dependent anion-selective channel in the presence of phospholipids. J. Struct. Biol. 127:1999;64-71.
    • (1999) J. Struct. Biol. , vol.127 , pp. 64-71
    • Dolder, M.1    Zeth, K.2    Tittmann, P.3    Gross, H.4    Welte, W.5    Wallimann, T.6
  • 51
    • 0032188847 scopus 로고    scopus 로고
    • Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins
    • Hill K., Model K., Ryan M.T., Dietmeier K., Martin F., Wagner R., Pfanner N. Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins. Nature. 395:1998;516-521.
    • (1998) Nature , vol.395 , pp. 516-521
    • Hill, K.1    Model, K.2    Ryan, M.T.3    Dietmeier, K.4    Martin, F.5    Wagner, R.6    Pfanner, N.7
  • 52
    • 0030787877 scopus 로고    scopus 로고
    • Isolation and characterization of an amino acid-selective channel protein present in the chloroplastic outer envelope membrane
    • Pohlmayer K., Soll J., Steinkamp T., Hinnah S., Wagner R. Isolation and characterization of an amino acid-selective channel protein present in the chloroplastic outer envelope membrane. Proc. Natl. Acad. Sci. U. S. A. 94:1997;9504-9509.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9504-9509
    • Pohlmayer, K.1    Soll, J.2    Steinkamp, T.3    Hinnah, S.4    Wagner, R.5
  • 53
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux B., Walker J.E. Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260:1996;289-298.
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 54
    • 0033048415 scopus 로고    scopus 로고
    • The C-terminal half of RNase E, which organizes the Escherichia coli degradosome, participates in mRNA degradation but not rRNA processing in vivo
    • Lopez P.J., Marchand I., Joyce S.A., Dreyfus M. The C-terminal half of RNase E, which organizes the Escherichia coli degradosome, participates in mRNA degradation but not rRNA processing in vivo. Mol. Microbiol. 33:1999;188-199.
    • (1999) Mol. Microbiol. , vol.33 , pp. 188-199
    • Lopez, P.J.1    Marchand, I.2    Joyce, S.A.3    Dreyfus, M.4
  • 55
    • 0032855077 scopus 로고    scopus 로고
    • Inhibition of aggregation side reactions during in vitro protein folding
    • De Bernadez-Clark E., Schwarz E., Rudolph R. Inhibition of aggregation side reactions during in vitro protein folding. Methods Enzymol. 309:1999;217-236.
    • (1999) Methods Enzymol. , vol.309 , pp. 217-236
    • De Bernadez-Clark, E.1    Schwarz, E.2    Rudolph, R.3
  • 56
    • 0035997027 scopus 로고    scopus 로고
    • The chloroplast protein import channel Toc75: Pore properties and interaction with transit peptides
    • Hinnah S.C., Wagner R., Sveshnikova N., Harrer R., Soll J. The chloroplast protein import channel Toc75: pore properties and interaction with transit peptides. Biophys. J. 83:2002;899-911.
    • (2002) Biophys. J. , vol.83 , pp. 899-911
    • Hinnah, S.C.1    Wagner, R.2    Sveshnikova, N.3    Harrer, R.4    Soll, J.5
  • 58
    • 0035783023 scopus 로고    scopus 로고
    • Stability of membrane proteins: Relevance for the selection of appropriate methods for high-resolution structure determinations
    • Rosenbusch J.P. Stability of membrane proteins: relevance for the selection of appropriate methods for high-resolution structure determinations. J. Struct. Biol. 136:2001;144-157.
    • (2001) J. Struct. Biol. , vol.136 , pp. 144-157
    • Rosenbusch, J.P.1
  • 59
    • 0031010621 scopus 로고    scopus 로고
    • A method for assessing the stability of a membrane protein
    • Lau F.W., Bowie J.U. A method for assessing the stability of a membrane protein. Biochemistry. 36:1997;5884-5892.
    • (1997) Biochemistry , vol.36 , pp. 5884-5892
    • Lau, F.W.1    Bowie, J.U.2
  • 60
    • 0032810904 scopus 로고    scopus 로고
    • Overexpression of a designed 2.2 kb gene of eukaryotic phenylalanine ammonia-lyase in Escherichia coli
    • Baedeker M., Schulz G.E. Overexpression of a designed 2.2 kb gene of eukaryotic phenylalanine ammonia-lyase in Escherichia coli. FEBS Lett. 457:1999;57-60.
    • (1999) FEBS Lett. , vol.457 , pp. 57-60
    • Baedeker, M.1    Schulz, G.E.2
  • 61
    • 0030891856 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of squalene-hopene cyclase from Alicyclobacillus acidocaldarius
    • Wendt K.-U., Feil C., Lenhart A., Poralla K., Schulz G.E. Crystallization and preliminary X-ray crystallographic analysis of squalene-hopene cyclase from Alicyclobacillus acidocaldarius. Protein Sci. 6:1997;722-724.
    • (1997) Protein Sci. , vol.6 , pp. 722-724
    • Wendt, K.-U.1    Feil, C.2    Lenhart, A.3    Poralla, K.4    Schulz, G.E.5
  • 63
    • 0034610266 scopus 로고    scopus 로고
    • Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: Thermostability and electron transfer
    • Nogi T., Fathir I., Kobayashi M., Nozawa T., Miki K. Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer. Proc. Natl. Acad. Sci. U. S. A. 97:2000;13561-13566.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 13561-13566
    • Nogi, T.1    Fathir, I.2    Kobayashi, M.3    Nozawa, T.4    Miki, K.5
  • 64
    • 0015402568 scopus 로고
    • The upper temperature limit for eukaryotic organisms
    • Tansey M.R., Brock T.D. The upper temperature limit for eukaryotic organisms. Proc. Natl. Acad. Sci. U. S. A. 69:1972;2426-2428.
    • (1972) Proc. Natl. Acad. Sci. U. S. A. , vol.69 , pp. 2426-2428
    • Tansey, M.R.1    Brock, T.D.2
  • 65
    • 0032832765 scopus 로고    scopus 로고
    • Outer membrane protein A of E. coli folds into detergent micelles, but not in the presence of monomeric detergent
    • Kleinschmidt J.H., Wiener M.C., Tamm L.K. Outer membrane protein A of E. coli folds into detergent micelles, but not in the presence of monomeric detergent. Protein Sci. 8:1999;2065-2071.
    • (1999) Protein Sci. , vol.8 , pp. 2065-2071
    • Kleinschmidt, J.H.1    Wiener, M.C.2    Tamm, L.K.3
  • 66
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schägger H., von Jagow G. Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 199:1991;223-231.
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schägger, H.1    Von Jagow, G.2
  • 67
    • 0025218116 scopus 로고
    • Solubility as a function of protein structure and solvent components
    • Schein C.H. Solubility as a function of protein structure and solvent components. Bio/Technology. 8:1990;308-316.
    • (1990) Bio/Technology , vol.8 , pp. 308-316
    • Schein, C.H.1
  • 68
    • 0034707086 scopus 로고    scopus 로고
    • Interaction of membrane proteins and lipids with solubilizing detergents
    • le Maire M., Champeil P., Møller J.V. Interaction of membrane proteins and lipids with solubilizing detergents. Biochim. Biophys. Acta. 1508:2000;86-111.
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 86-111
    • Le Maire, M.1    Champeil, P.2    Møller, J.V.3
  • 69
    • 0032726068 scopus 로고    scopus 로고
    • Renaturation of recombinant Treponema pallidum rare outer membrane protein 1 into a trimeric hydrophobic, and porin-active conformation
    • Zhang H.H., Blanco D.R., Exner M.M., Shang E.S., Champion C.I., Phillips M.L., Miller J.N., Lovett M.A. Renaturation of recombinant Treponema pallidum rare outer membrane protein 1 into a trimeric hydrophobic, and porin-active conformation. J. Bacteriol. 181:1999;7168-7175.
    • (1999) J. Bacteriol. , vol.181 , pp. 7168-7175
    • Zhang, H.H.1    Blanco, D.R.2    Exner, M.M.3    Shang, E.S.4    Champion, C.I.5    Phillips, M.L.6    Miller, J.N.7    Lovett, M.A.8
  • 70
    • 0031471216 scopus 로고    scopus 로고
    • Overexpression of a glutamate receptor (GluR2) ligand binding domain in Escherichia coli: Application of a novel protein folding screen
    • Chen G.-Q., Gouaux E. Overexpression of a glutamate receptor (GluR2) ligand binding domain in Escherichia coli: application of a novel protein folding screen. Proc. Natl. Acad. Sci. U. S. A. 94:1997;13431-13436.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 13431-13436
    • Chen, G.-Q.1    Gouaux, E.2
  • 72
    • 0026660841 scopus 로고
    • Protein compositional analysis of inclusion bodies produced in recombinant Escherichia coli
    • Rinas U., Bailey J.E. Protein compositional analysis of inclusion bodies produced in recombinant Escherichia coli. Appl. Microbiol. Biotechnol. 37:1992;609-614.
    • (1992) Appl. Microbiol. Biotechnol. , vol.37 , pp. 609-614
    • Rinas, U.1    Bailey, J.E.2
  • 73
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson A.D., Hofmann E., Coulton J.W., Diederichs K., Welte W. Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science. 282:1998;2215-2220.
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 74
    • 0028153088 scopus 로고
    • Refined structure of the porin from Rhodopseudomonas blastica and comparison with the porin from Rhodobacter capsulatus
    • Kreusch A., Schulz G.E. Refined structure of the porin from Rhodopseudomonas blastica and comparison with the porin from Rhodobacter capsulatus. J. Mol. Biol. 243:1994;891-905.
    • (1994) J. Mol. Biol. , vol.243 , pp. 891-905
    • Kreusch, A.1    Schulz, G.E.2
  • 76
    • 0034724567 scopus 로고    scopus 로고
    • High resolution structure of the OmpA membrane domain
    • Pautsch A., Schulz G.E. High resolution structure of the OmpA membrane domain. J. Mol. Biol. 298:2000;273-282.
    • (2000) J. Mol. Biol. , vol.298 , pp. 273-282
    • Pautsch, A.1    Schulz, G.E.2
  • 77
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution
    • Schirmer T., Keller T.A., Wang Y.-F., Rosenbusch J.P. Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution. Science. 267:1995;512-514.
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.A.2    Wang, Y.-F.3    Rosenbusch, J.P.4
  • 78
    • 0031985785 scopus 로고    scopus 로고
    • Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose
    • Forst D., Welte W., Wacker T., Diederichs K. Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose. Nat. Struct. Biol. 5:1998;37-46.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 37-46
    • Forst, D.1    Welte, W.2    Wacker, T.3    Diederichs, K.4
  • 79
    • 0032414254 scopus 로고    scopus 로고
    • Transmembrane signaling across the ligand-gated FhuA receptor: Crystal structures of free and ferrichrome-bound states reveal allosteric changes
    • Locher K.P., Rees B., Koebnik R., Mitschler A., Moulinier L., Rosenbusch J.P., Moras D. Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes. Cell. 95:1998;771-778.
    • (1998) Cell , vol.95 , pp. 771-778
    • Locher, K.P.1    Rees, B.2    Koebnik, R.3    Mitschler, A.4    Moulinier, L.5    Rosenbusch, J.P.6    Moras, D.7
  • 81
    • 0034660537 scopus 로고    scopus 로고
    • A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins
    • Ferguson A.D., Welte W., Hofmann E., Lindner B., Holst O., Coulton J.W., Diederichs K. A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins. Structure. 8:2000;585-592.
    • (2000) Structure , vol.8 , pp. 585-592
    • Ferguson, A.D.1    Welte, W.2    Hofmann, E.3    Lindner, B.4    Holst, O.5    Coulton, J.W.6    Diederichs, K.7
  • 82
    • 0034665240 scopus 로고    scopus 로고
    • Crystal structures of Omp32, the anion-selective porin from Comamonas acidovorans, in complex with a periplasmic peptide at 2.1 Å resolution
    • Zeth K., Diederichs K., Welte W., Engelhardt H. Crystal structures of Omp32, the anion-selective porin from Comamonas acidovorans, in complex with a periplasmic peptide at 2.1 Å resolution. Structure. 8:2000;981-992.
    • (2000) Structure , vol.8 , pp. 981-992
    • Zeth, K.1    Diederichs, K.2    Welte, W.3    Engelhardt, H.4
  • 83
    • 0034629489 scopus 로고    scopus 로고
    • Building a thermostable membrane protein
    • Zhou Y., Bowie J.U. Building a thermostable membrane protein. J. Biol. Chem. 275:2000;6975-6979.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6975-6979
    • Zhou, Y.1    Bowie, J.U.2
  • 84
    • 0022558545 scopus 로고
    • Isolation and crystallization of bacterial porin
    • Garavito M., Rosenbusch J.R. Isolation and crystallization of bacterial porin. Methods Enzymol. 125:1986;309-328.
    • (1986) Methods Enzymol. , vol.125 , pp. 309-328
    • Garavito, M.1    Rosenbusch, J.R.2
  • 88
    • 0028800276 scopus 로고
    • Purification, characterization, crystallization, and preliminary X-ray results from Paracoccus denitrificans porin
    • Hirsch A., Wacker T., Weckesser J., Diederichs K., Welte W. Purification, characterization, crystallization, and preliminary X-ray results from Paracoccus denitrificans porin. Proteins: Struct. Funct. Genet. 23:1995;282-284.
    • (1995) Proteins: Struct. Funct. Genet. , vol.23 , pp. 282-284
    • Hirsch, A.1    Wacker, T.2    Weckesser, J.3    Diederichs, K.4    Welte, W.5
  • 89
    • 0032128128 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic studies of the native and chemically modified anion-selective porin from Comamonas acidovorans
    • Zeth K., Schnaible V., Przybylski M., Welte W., Diederichs K., Engelhardt H. Crystallization and preliminary X-ray crystallographic studies of the native and chemically modified anion-selective porin from Comamonas acidovorans. Acta Crystallogr., D. 54:1998;650-653.
    • (1998) Acta Crystallogr., D , vol.54 , pp. 650-653
    • Zeth, K.1    Schnaible, V.2    Przybylski, M.3    Welte, W.4    Diederichs, K.5    Engelhardt, H.6
  • 90
    • 0031733336 scopus 로고    scopus 로고
    • Structure of outer membrane protein A transmembrane domain
    • Pautsch A., Schulz G.E. Structure of outer membrane protein A transmembrane domain. Nat. Struct. Biol. 5:1999;1013-1017.
    • (1999) Nat. Struct. Biol. , vol.5 , pp. 1013-1017
    • Pautsch, A.1    Schulz, G.E.2
  • 91
    • 0033570111 scopus 로고    scopus 로고
    • Structure of the outer membrane protein OmpX from Escherichia coli
    • Vogt J., Schulz G.E. Structure of the outer membrane protein OmpX from Escherichia coli. Structure. 7:1999;1301-1309.
    • (1999) Structure , vol.7 , pp. 1301-1309
    • Vogt, J.1    Schulz, G.E.2
  • 93
    • 0037133637 scopus 로고    scopus 로고
    • Crystal structure of the OpcA integral membrane adhesin from Neisseria meningitidis
    • Prince S.M., Achtman M., Derrick J.P. Crystal structure of the OpcA integral membrane adhesin from Neisseria meningitidis. Proc. Natl. Acad. Sci. U. S. A. 99:2002;3417-3421.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 3417-3421
    • Prince, S.M.1    Achtman, M.2    Derrick, J.P.3
  • 94
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
    • Song L., Hobaugh M.R., Shustak C., Cheley S., Bayley H., Gouaux J.E. Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore. Science. 274:1996;1859-1866.
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.