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Volumn 922, Issue , 2012, Pages 123-131

Structural studies of SSB interaction with RecO

Author keywords

Atomic resolution structure; DNA recombination and repair; Fluorescence polarization; Peptide binding; Protein crystallization; Selenomethionine protein derivative

Indexed keywords

DNA BINDING PROTEIN; RECO PROTEIN;

EID: 84934441831     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-62703-32-8_7     Document Type: Article
Times cited : (13)

References (16)
  • 1
    • 33847795537 scopus 로고    scopus 로고
    • Regulation of bacterial RecA protein function
    • Cox MM (2007) Regulation of bacterial RecA protein function. Crit Rev Biochem Mol Biol 42(1):41-63
    • (2007) Crit Rev Biochem Mol Biol , vol.42 , Issue.1 , pp. 41-63
    • Cox, M.M.1
  • 2
    • 0027238208 scopus 로고
    • Biochemical interaction of the Escherichia coli RecF, RecO, and RecR proteins with RecA protein and single-stranded DNA binding protein
    • Umezu K, Chi NW, Kolodner RD (1993) Biochemical interaction of the Escherichia coli RecF, RecO, and RecR proteins with RecA protein and single-stranded DNA binding protein. Proc Natl Acad Sci USA 90 (9):3875-3879
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.9 , pp. 3875-3879
    • Umezu, K.1    Chi, N.W.2    Kolodner, R.D.3
  • 3
    • 59149085483 scopus 로고    scopus 로고
    • RecFOR and RecOR as distinct RecA loading pathways
    • Sakai A, CoxMM(2009) RecFOR and RecOR as distinct RecA loading pathways. J Biol Chem 284(5):3264-3272
    • (2009) J Biol Chem , vol.284 , Issue.5 , pp. 3264-3272
    • Sakai, A.1    Cox, M.M.2
  • 4
    • 0033939135 scopus 로고    scopus 로고
    • Controlled intracellular processing of fusion proteins by TEV protease
    • Kapust RB,Waugh DS (2000) Controlled intracellular processing of fusion proteins by TEV protease. Protein Expr Purif 19(2):312-318
    • (2000) Protein Expr Purif , vol.19 , Issue.2 , pp. 312-318
    • Kapust, R.B.1    Waugh, D.S.2
  • 5
    • 0036926615 scopus 로고    scopus 로고
    • A new vector for highthroughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site
    • Stols L et al (2002) A new vector for highthroughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site. Protein Expr Purif 25:8-15
    • (2002) Protein Expr Purif , vol.25 , pp. 8-15
    • Stols, L..1
  • 6
    • 4644266683 scopus 로고    scopus 로고
    • A novel structure of DNA repair protein RecO from Deinococcus radiodurans
    • Makharashvili N, Koroleva O, Bera S, Grandgenett DP, Korolev S (2004) A novel structure of DNA repair protein RecO from Deinococcus radiodurans. Structure 12 (10):1881-1889
    • (2004) Structure , vol.12 , Issue.10 , pp. 1881-1889
    • Makharashvili, N.1    Koroleva, O.2    Bera, S.3    Grandgenett, D.P.4    Korolev, S.5
  • 8
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethioninyl proteins for phase determination
    • Doublie S (1997) Preparation of selenomethioninyl proteins for phase determination. Methods Enzymol 276:523-530
    • (1997) Methods Enzymol , vol.276 , pp. 523-530
    • Doublie, S.1
  • 9
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 10
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy AJ et al (2007) Phaser crystallographic software. J Appl Crystallogr 40(Pt 4):658-674
    • (2007) J Appl Crystallogr , vol.40 , Issue.PART 4 , pp. 658-674
    • McCoy, A.J..1
  • 11
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD et al (2010) PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2):213-221
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.PART 2 , pp. 213-221
    • Adams, P.D..1
  • 12
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer G, Cohen SX, Lamzin VS, Perrakis A (2008) Automated macromolecular model building for X-ray crystallography using ARP/ wARP version 7. Nat Protoc 3(7):1171-1179
    • (2008) Nat Protoc , vol.3 , Issue.7 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 14
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS refinement in REFMAC at moderate resolutions
    • Winn MD, Murshudov GN, Papiz MZ (2003) Macromolecular TLS refinement in REFMAC at moderate resolutions. Methods Enzymol 374:300-321
    • (2003) Methods Enzymol , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshudov, G.N.2    Papiz, M.Z.3
  • 15
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the Crystallography and NMR system
    • Brunger AT (2007) Version 1.2 of the Crystallography and NMR system. Nat Protoc 2 (11):2728-2733
    • (2007) Nat Protoc , vol.2 , Issue.11 , pp. 2728-2733
    • Brunger, A.T.1
  • 16
    • 0033954256 scopus 로고    scopus 로고
    • The protein data bank
    • Berman HM et al (2000) The Protein Data Bank. Nucleic Acids Res 28(1):235-242
    • (2000) Nucleic Acids Res , vol.28 , Issue.1 , pp. 235-242
    • Berman, H.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.