메뉴 건너뛰기




Volumn 40, Issue 2, 2005, Pages 256-267

Protocols for production of selenomethionine-labeled proteins in 2-L polyethylene terephthalate bottles using auto-induction medium

Author keywords

Auto induction; Cell growth; Polyethylene terephthalate; Selenomethionine

Indexed keywords


EID: 20044376278     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2004.12.022     Document Type: Article
Times cited : (101)

References (31)
  • 1
    • 0031056818 scopus 로고    scopus 로고
    • Overview of isomorphous replacement phasing
    • H. Ke Overview of isomorphous replacement phasing Methods Enzymol. 276 1997 448 461
    • (1997) Methods Enzymol. , vol.276 , pp. 448-461
    • Ke, H.1
  • 2
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • S. Doublie Preparation of selenomethionyl proteins for phase determination Methods Enzymol. 276 1997 523 530
    • (1997) Methods Enzymol. , vol.276 , pp. 523-530
    • Doublie, S.1
  • 3
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • W.A. Hendrickson, J.R. Horton, and D.M. LeMaster Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure EMBO J. 9 1990 1665 1672
    • (1990) EMBO J. , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    Lemaster, D.M.3
  • 4
    • 0032536841 scopus 로고    scopus 로고
    • Spontaneous cAMP-dependent derepression of gene expression in stationary phase plays a role in recombinant expression instability
    • T.H. Grossman, E.S. Kawasaki, S.R. Punreddy, and M.S. Osburne Spontaneous cAMP-dependent derepression of gene expression in stationary phase plays a role in recombinant expression instability Gene 209 1998 95 103
    • (1998) Gene , vol.209 , pp. 95-103
    • Grossman, T.H.1    Kawasaki, E.S.2    Punreddy, S.R.3    Osburne, M.S.4
  • 5
    • 0033152987 scopus 로고    scopus 로고
    • Application of fed-batch fermentation to the preparation of isotopically labeled- or selenomethionine-labeled proteins
    • J.M. Studts, and B.G. Fox Application of fed-batch fermentation to the preparation of isotopically labeled- or selenomethionine-labeled proteins Protein Expr. Purif. 16 1999 109 119
    • (1999) Protein Expr. Purif. , vol.16 , pp. 109-119
    • Studts, J.M.1    Fox, B.G.2
  • 6
    • 3543110895 scopus 로고    scopus 로고
    • Production of selenomethionine-labeled proteins in two-liter plastic bottles for structure determination
    • L. Stols, C. Sanville Millard, I. Dementieva, and M.I. Donnelly Production of selenomethionine-labeled proteins in two-liter plastic bottles for structure determination J. Struct. Funct. Genom. 5 2003 95 102
    • (2003) J. Struct. Funct. Genom. , vol.5 , pp. 95-102
    • Stols, L.1    Sanville Millard, C.2    Dementieva, I.3    Donnelly, M.I.4
  • 7
    • 0014571087 scopus 로고
    • Some chemical and biochemical properties of selenomethionine
    • L. Shepherd, and R.E. Huber Some chemical and biochemical properties of selenomethionine Can. J. Biochem. 47 1969 877 881
    • (1969) Can. J. Biochem. , vol.47 , pp. 877-881
    • Shepherd, L.1    Huber, R.E.2
  • 8
    • 0037790957 scopus 로고    scopus 로고
    • A less laborious approach to the high-throughput production of recombinant proteins in Escherichia coli using 2-liter plastic bottles
    • C. Sanville Millard, L. Stols, P. Quartey, Y. Kim, I. Dementieva, and M.I. Donnelly A less laborious approach to the high-throughput production of recombinant proteins in Escherichia coli using 2-liter plastic bottles Protein Expr. Purif. 29 2003 311 320
    • (2003) Protein Expr. Purif. , vol.29 , pp. 311-320
    • Sanville Millard, C.1    Stols, L.2    Quartey, P.3    Kim, Y.4    Dementieva, I.5    Donnelly, M.I.6
  • 13
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high-density shaking cultures
    • (in press)
    • F.W. Studier, Protein production by auto-induction in high-density shaking cultures, Protein Expr. Purif. (2005) (in press)
    • (2005) Protein Expr. Purif.
    • Studier, F.W.1
  • 14
    • 10844238943 scopus 로고    scopus 로고
    • Unattended high-density cell growth and induction of protein expression with the overnight express TM autoinduction system
    • A. Grabski, M. Mehler, and D. Drott Unattended high-density cell growth and induction of protein expression with the overnight express TM autoinduction system Innovations 17 2003 3 6
    • (2003) Innovations , vol.17 , pp. 3-6
    • Grabski, A.1    Mehler, M.2    Drott, D.3
  • 18
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • R.B. Kapust, and D.S. Waugh Escherichia coli maltose binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused Protein Sci. 8 1999 1668 1674
    • (1999) Protein Sci. , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 20
    • 0027251273 scopus 로고
    • Physical mapping of scattered methionine genes on the Escherichia coli chromosome
    • I.G. Old, I.S. Girons, and C. Richaud Physical mapping of scattered methionine genes on the Escherichia coli chromosome J. Bacteriol. 175 1993 3689 3691
    • (1993) J. Bacteriol. , vol.175 , pp. 3689-3691
    • Old, I.G.1    Girons, I.S.2    Richaud, C.3
  • 21
    • 0020374667 scopus 로고
    • Mutations affecting regulation of methionine biosynthetic genes isolated by use of met-lac fusions
    • J.T. Mulligan, W. Margolin, J.H. Krueger, and G.C. Walker Mutations affecting regulation of methionine biosynthetic genes isolated by use of met-lac fusions J. Bacteriol. 151 1982 609 619
    • (1982) J. Bacteriol. , vol.151 , pp. 609-619
    • Mulligan, J.T.1    Margolin, W.2    Krueger, J.H.3    Walker, G.C.4
  • 23
    • 0027513392 scopus 로고
    • Effects of consecutive AGG codons on translation in Escherichia coli, demonstrated with a versatile codon test system
    • A.H. Rosenberg, E. Goldman, J.J. Dunn, F.W. Studier, and G. Zubay Effects of consecutive AGG codons on translation in Escherichia coli, demonstrated with a versatile codon test system J. Bacteriol. 175 1993 716 722
    • (1993) J. Bacteriol. , vol.175 , pp. 716-722
    • Rosenberg, A.H.1    Goldman, E.2    Dunn, J.J.3    Studier, F.W.4    Zubay, G.5
  • 24
    • 0027960812 scopus 로고
    • Role of the AGA/AGG codons, the rarest codons in global gene expression in Escherichia coli
    • G.T. Chen, and M. Inouye Role of the AGA/AGG codons, the rarest codons in global gene expression in Escherichia coli Genes Dev 8 1994 2641 2652
    • (1994) Genes Dev , vol.8 , pp. 2641-2652
    • Chen, G.T.1    Inouye, M.2
  • 25
    • 0028804911 scopus 로고
    • Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli
    • J.F. Kane Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli Curr. Opin. Biotechnol. 6 1995 494 500
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 494-500
    • Kane, J.F.1
  • 27
    • 0037426342 scopus 로고    scopus 로고
    • In vitro studies of transcript initiation by Escherichia coli RNA polymerase. 1. RNA chain initiation, abortive initiation, and promoter escape at three bacteriophage promoters
    • L.M. Hsu, N.V. Vo, C.M. Kane, and M.J. Chamberlin In vitro studies of transcript initiation by Escherichia coli RNA polymerase. 1. RNA chain initiation, abortive initiation, and promoter escape at three bacteriophage promoters Biochemistry 42 2003 3777 3786
    • (2003) Biochemistry , vol.42 , pp. 3777-3786
    • Hsu, L.M.1    Vo, N.V.2    Kane, C.M.3    Chamberlin, M.J.4
  • 29
    • 0026510132 scopus 로고
    • Maximizing the expression of a recombinant gene in Escherichia coli by manipulation of induction time using lactose as an inducer
    • P. Neubauer, K. Hofmann, O. Holst, B. Mattiasson, and P. Kruschke Maximizing the expression of a recombinant gene in Escherichia coli by manipulation of induction time using lactose as an inducer Appl. Microbiol. Biotechnol. 36 1992 739 744
    • (1992) Appl. Microbiol. Biotechnol. , vol.36 , pp. 739-744
    • Neubauer, P.1    Hofmann, K.2    Holst, O.3    Mattiasson, B.4    Kruschke, P.5
  • 30
    • 0029379752 scopus 로고
    • Lactose fed-batch overexpression of recombinant metalloproteins in Escherichia coli BL21(DE3): Process control yielding high levels of metal incorporated, soluble protein
    • B.J. Hoffman, J.A. Broadwater, P. Johnson, J. Harper, B.G. Fox, and W.R. Kenealy Lactose fed-batch overexpression of recombinant metalloproteins in Escherichia coli BL21(DE3): Process control yielding high levels of metal incorporated, soluble protein Protein Expr. Purif. 6 1995 646 654
    • (1995) Protein Expr. Purif. , vol.6 , pp. 646-654
    • Hoffman, B.J.1    Broadwater, J.A.2    Johnson, P.3    Harper, J.4    Fox, B.G.5    Kenealy, W.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.