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Volumn 5, Issue 12, 2009, Pages

Three dimensional structure of the MqsR:MqsA complex: A novel TA pair comprised of a toxin homologous to RelE and an antitoxin with unique properties

Author keywords

[No Author keywords available]

Indexed keywords

ANTITOXIN; BACTERIAL DNA; BACTERIAL TOXIN; HELIX LOOP HELIX PROTEIN; MQSA ANTITOXIN; RELE TOXIN; RIBONUCLEASE; UNCLASSIFIED DRUG; YOEB TOXIN; ESCHERICHIA COLI PROTEIN; MQSR PROTEIN, E COLI;

EID: 74549170423     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1000706     Document Type: Article
Times cited : (148)

References (61)
  • 1
    • 50349141358 scopus 로고
    • Treatment of staphylococcal infections with penicillin
    • Bigger JW (1944) Treatment of staphylococcal infections with penicillin. Lancet. pp 497-500.
    • (1944) Lancet , pp. 497-500
    • Bigger, J.W.1
  • 2
    • 10044266575 scopus 로고    scopus 로고
    • Specialized persister cells and the mechanism of multidrug tolerance in Escherichia coli
    • Keren I, Shah D, Spoering A, Kaldalu N, Lewis K (2004) Specialized persister cells and the mechanism of multidrug tolerance in Escherichia coli. J Bacteriol 186: 8172-8180.
    • (2004) J Bacteriol , vol.186 , pp. 8172-8180
    • Keren, I.1    Shah, D.2    Spoering, A.3    Kaldalu, N.4    Lewis, K.5
  • 4
    • 0025940779 scopus 로고
    • Structure and organization of hip, an operon that affects lethality due to inhibition of peptidoglycan or DNA synthesis
    • Black DS, Kelly AJ, Mardis MJ, Moyed HS (1991) Structure and organization of hip, an operon that affects lethality due to inhibition of peptidoglycan or DNA synthesis. J Bacteriol 173: 5732-5739.
    • (1991) J Bacteriol , vol.173 , pp. 5732-5739
    • Black, D.S.1    Kelly, A.J.2    Mardis, M.J.3    Moyed, H.S.4
  • 5
    • 0035173818 scopus 로고    scopus 로고
    • Biofilms and planktonic cells of Pseudomonas aeruginosa have similar resistance to killing by antimicrobials
    • Spoering AL, Lewis K (2001) Biofilms and planktonic cells of Pseudomonas aeruginosa have similar resistance to killing by antimicrobials. J Bacteriol 183: 6746-6751.
    • (2001) J Bacteriol , vol.183 , pp. 6746-6751
    • Spoering, A.L.1    Lewis, K.2
  • 8
    • 34548488930 scopus 로고    scopus 로고
    • Hypothetical functions of toxin-antitoxin systems
    • Magnuson RD (2007) Hypothetical functions of toxin-antitoxin systems. J Bacteriol 189: 6089-6092.
    • (2007) J Bacteriol , vol.189 , pp. 6089-6092
    • Magnuson, R.D.1
  • 9
    • 0345333119 scopus 로고
    • Unique type of plasmid maintenance function: Postsegregational killing of plasmid-free cells
    • Gerdes K, Rasmussen PB, Molin S (1986) Unique type of plasmid maintenance function: postsegregational killing of plasmid-free cells. Proc Natl Acad Sci U S A 83: 3116-3120.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 3116-3120
    • Gerdes, K.1    Rasmussen, P.B.2    Molin, S.3
  • 10
    • 0020804285 scopus 로고
    • Mini-F plasmid genes that couple host cell division to plasmid proliferation
    • Ogura T, Hiraga S (1983) Mini-F plasmid genes that couple host cell division to plasmid proliferation. Proc Natl Acad Sci U S A 80: 4784-4788.
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 4784-4788
    • Ogura, T.1    Hiraga, S.2
  • 11
    • 0030008368 scopus 로고    scopus 로고
    • An Escherichia coli chromosomal "addiction module" regulated by guanosine [corrected] 3′,5′-bispyrophosphate: A model for programmed bacterial cell death
    • Aizenman E, Engelberg-Kulka H, Glaser G (1996) An Escherichia coli chromosomal "addiction module" regulated by guanosine [corrected] 3′,5′-bispyrophosphate: a model for programmed bacterial cell death. Proc Natl Acad Sci U S A 93: 6059-6063.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 6059-6063
    • Aizenman, E.1    Engelberg-Kulka, H.2    Glaser, G.3
  • 12
    • 0031816179 scopus 로고    scopus 로고
    • The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family
    • Gotfredsen M, Gerdes K (1998) The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family. Mol Microbiol 29: 1065-1076.
    • (1998) Mol Microbiol , vol.29 , pp. 1065-1076
    • Gotfredsen, M.1    Gerdes, K.2
  • 13
    • 0027522090 scopus 로고
    • chpA and chpB, Escherichia coli chromosomal homologs of the pem locus responsible for stable maintenance of plasmid R100
    • Masuda Y, Miyakawa K, Nishimura Y, Ohtsubo E (1993) chpA and chpB, Escherichia coli chromosomal homologs of the pem locus responsible for stable maintenance of plasmid R100. J Bacteriol 175: 6850-6856.
    • (1993) J Bacteriol , vol.175 , pp. 6850-6856
    • Masuda, Y.1    Miyakawa, K.2    Nishimura, Y.3    Ohtsubo, E.4
  • 14
    • 0037338682 scopus 로고    scopus 로고
    • Axe-Txe, a broad-spectrum proteic toxin-antitoxin system specified by a multidrug-resistant, clinical isolate of Enterococcus faecium
    • Grady R, Hayes F (2003) Axe-Txe, a broad-spectrum proteic toxin-antitoxin system specified by a multidrug-resistant, clinical isolate of Enterococcus faecium. Mol Microbiol 47: 1419-1432.
    • (2003) Mol Microbiol , vol.47 , pp. 1419-1432
    • Grady, R.1    Hayes, F.2
  • 15
    • 39149110856 scopus 로고    scopus 로고
    • RASTA-Bacteria: A web-based tool for identifying toxin-antitoxin loci in prokaryotes
    • Sevin EW, Barloy-Hubler F (2007) RASTA-Bacteria: a web-based tool for identifying toxin-antitoxin loci in prokaryotes. Genome Biol 8: R155.
    • (2007) Genome Biol , vol.8
    • Sevin, E.W.1    Barloy-Hubler, F.2
  • 16
    • 0028222452 scopus 로고
    • Lon-dependent proteolysis of CcdA is the key control for activation of CcdB in plasmid-free segregant bacteria
    • Van Melderen L, Bernard P, Couturier M (1994) Lon-dependent proteolysis of CcdA is the key control for activation of CcdB in plasmid-free segregant bacteria. Mol Microbiol 11: 1151-1157.
    • (1994) Mol Microbiol , vol.11 , pp. 1151-1157
    • Van Melderen, L.1    Bernard, P.2    Couturier, M.3
  • 17
    • 1642483754 scopus 로고    scopus 로고
    • Overproduction of the Lon protease triggers inhibition of translation in Escherichia coli: Involvement of the yefM-yoeB toxin-antitoxin system
    • Christensen SK, Maenhaut-Michel G, Mine N, Gottesman S, Gerdes K, et al. (2004) Overproduction of the Lon protease triggers inhibition of translation in Escherichia coli: involvement of the yefM-yoeB toxin-antitoxin system. Mol Microbiol 51: 1705-1717.
    • (2004) Mol Microbiol , vol.51 , pp. 1705-1717
    • Christensen, S.K.1    Maenhaut-Michel, G.2    Mine, N.3    Gottesman, S.4    Gerdes, K.5
  • 18
    • 0028985596 scopus 로고
    • Addiction protein Phd of plasmid prophage P1 is a substrate of the ClpXP serine protease of Escherichia coli
    • Lehnherr H, Yarmolinsky MB (1995) Addiction protein Phd of plasmid prophage P1 is a substrate of the ClpXP serine protease of Escherichia coli. Proc Natl Acad Sci U S A 92: 3274-3277.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 3274-3277
    • Lehnherr, H.1    Yarmolinsky, M.B.2
  • 20
    • 0036098378 scopus 로고    scopus 로고
    • ParE toxin encoded by the broad-host-range plasmid RK2 is an inhibitor of Escherichia coli gyrase
    • Jiang Y, Pogliano J, Helinski DR, Konieczny I (2002) ParE toxin encoded by the broad-host-range plasmid RK2 is an inhibitor of Escherichia coli gyrase. Mol Microbiol 44: 971-979.
    • (2002) Mol Microbiol , vol.44 , pp. 971-979
    • Jiang, Y.1    Pogliano, J.2    Helinski, D.R.3    Konieczny, I.4
  • 21
    • 0026735990 scopus 로고
    • Modulation of DNA supercoiling activity of Escherichia coli DNA gyrase by F plasmid proteins. Antagonistic actions of LetA (CcdA) and LetD (CcdB) proteins
    • Maki S, Takiguchi S, Miki T, Horiuchi T (1992) Modulation of DNA supercoiling activity of Escherichia coli DNA gyrase by F plasmid proteins. Antagonistic actions of LetA (CcdA) and LetD (CcdB) proteins. J Biol Chem 267: 12244-12251.
    • (1992) J Biol Chem , vol.267 , pp. 12244-12251
    • Maki, S.1    Takiguchi, S.2    Miki, T.3    Horiuchi, T.4
  • 22
    • 0041825422 scopus 로고    scopus 로고
    • Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA
    • Christensen SK, Pedersen K, Hansen FG, Gerdes K (2003) Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA. J Mol Biol 332: 809-819.
    • (2003) J Mol Biol , vol.332 , pp. 809-819
    • Christensen, S.K.1    Pedersen, K.2    Hansen, F.G.3    Gerdes, K.4
  • 23
    • 0037428226 scopus 로고    scopus 로고
    • The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site
    • Pedersen K, Zavialov AV, Pavlov MY, Elf J, Gerdes K, et al. (2003) The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site. Cell 112: 131-140.
    • (2003) Cell , vol.112 , pp. 131-140
    • Pedersen, K.1    Zavialov, A.V.2    Pavlov, M.Y.3    Elf, J.4    Gerdes, K.5
  • 24
    • 58449087611 scopus 로고    scopus 로고
    • Molecular mechanisms of HipA-mediated multidrug tolerance and its neutralization by HipB
    • Schumacher MA, Piro KM, Xu W, Hansen S, Lewis K, et al. (2009) Molecular mechanisms of HipA-mediated multidrug tolerance and its neutralization by HipB. Science 323: 396-401.
    • (2009) Science , vol.323 , pp. 396-401
    • Schumacher, M.A.1    Piro, K.M.2    Xu, W.3    Hansen, S.4    Lewis, K.5
  • 25
    • 0024730408 scopus 로고
    • Autoregulation of the ccd operon in the F plasmid
    • de Feyter R, Wallace C, Lane D (1989) Autoregulation of the ccd operon in the F plasmid. Mol Gen Genet 218: 481-486.
    • (1989) Mol Gen Genet , vol.218 , pp. 481-486
    • de Feyter, R.1    Wallace, C.2    Lane, D.3
  • 26
    • 0031785682 scopus 로고    scopus 로고
    • Corepression of the P1 addiction operon by Phd and Doc
    • Magnuson R, Yarmolinsky MB (1998) Corepression of the P1 addiction operon by Phd and Doc. J Bacteriol 180: 6342-6351.
    • (1998) J Bacteriol , vol.180 , pp. 6342-6351
    • Magnuson, R.1    Yarmolinsky, M.B.2
  • 27
    • 0024747885 scopus 로고
    • The F plasmid ccd autorepressor is a complex of CcdA and CcdB proteins
    • Tam JE, Kline BC (1989) The F plasmid ccd autorepressor is a complex of CcdA and CcdB proteins. Mol Gen Genet 219: 26-32.
    • (1989) Mol Gen Genet , vol.219 , pp. 26-32
    • Tam, J.E.1    Kline, B.C.2
  • 28
    • 18744409067 scopus 로고    scopus 로고
    • Crystal structure of archaeal toxin-antitoxin RelE-RelB complex with implications for toxin activity and antitoxin effects
    • Takagi H, Kakuta Y, Okada T, Yao M, Tanaka I, et al. (2005) Crystal structure of archaeal toxin-antitoxin RelE-RelB complex with implications for toxin activity and antitoxin effects. Nat Struct Mol Biol 12: 327-331.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 327-331
    • Takagi, H.1    Kakuta, Y.2    Okada, T.3    Yao, M.4    Tanaka, I.5
  • 29
    • 0037738520 scopus 로고    scopus 로고
    • Crystal structure of the MazE/MazF complex: Molecular bases of antidote-toxin recognition
    • Kamada K, Hanaoka F, Burley SK (2003) Crystal structure of the MazE/MazF complex: molecular bases of antidote-toxin recognition. Mol Cell 11: 875-884.
    • (2003) Mol Cell , vol.11 , pp. 875-884
    • Kamada, K.1    Hanaoka, F.2    Burley, S.K.3
  • 31
    • 0028270774 scopus 로고
    • Autoregulation of hip, an operon that affects lethality due to inhibition of peptidoglycan or DNA synthesis
    • Black DS, Irwin B, Moyed HS (1994) Autoregulation of hip, an operon that affects lethality due to inhibition of peptidoglycan or DNA synthesis. J Bacteriol 176: 4081-4091.
    • (1994) J Bacteriol , vol.176 , pp. 4081-4091
    • Black, D.S.1    Irwin, B.2    Moyed, H.S.3
  • 32
    • 60849121408 scopus 로고    scopus 로고
    • HicA of Escherichia coli defines a novel family of translation-independent mRNA interferases in bacteria and archaea
    • Jorgensen MG, Pandey DP, Jaskolska M, Gerdes K (2009) HicA of Escherichia coli defines a novel family of translation-independent mRNA interferases in bacteria and archaea. J Bacteriol 191: 1191-1199.
    • (2009) J Bacteriol , vol.191 , pp. 1191-1199
    • Jorgensen, M.G.1    Pandey, D.P.2    Jaskolska, M.3    Gerdes, K.4
  • 33
    • 23744463273 scopus 로고    scopus 로고
    • Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin
    • Kamada K, Hanaoka F (2005) Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin. Mol Cell 19: 497-509.
    • (2005) Mol Cell , vol.19 , pp. 497-509
    • Kamada, K.1    Hanaoka, F.2
  • 34
    • 30744444010 scopus 로고    scopus 로고
    • Autoinducer 2 controls biofilm formation in Escherichia coli through a novel motility quorum-sensing regulator (MqsR, B3022)
    • Gonzalez Barrios AF, Zuo R, Hashimoto Y, Yang L, Bentley WE, et al. (2006) Autoinducer 2 controls biofilm formation in Escherichia coli through a novel motility quorum-sensing regulator (MqsR, B3022). J Bacteriol 188: 305-316.
    • (2006) J Bacteriol , vol.188 , pp. 305-316
    • Gonzalez Barrios, A.F.1    Zuo, R.2    Hashimoto, Y.3    Yang, L.4    Bentley, W.E.5
  • 36
    • 31544450286 scopus 로고    scopus 로고
    • Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, et al. (2006) Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol Syst Biol 2: 2006.0008.
    • Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, et al. (2006) Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol Syst Biol 2: 2006.0008.
  • 37
    • 33749178742 scopus 로고    scopus 로고
    • Two higBA loci in the Vibrio cholerae superintegron encode mRNA cleaving enzymes and can stabilize plasmids
    • Christensen-Dalsgaard M, Gerdes K (2006) Two higBA loci in the Vibrio cholerae superintegron encode mRNA cleaving enzymes and can stabilize plasmids. Mol Microbiol 62: 397-411.
    • (2006) Mol Microbiol , vol.62 , pp. 397-411
    • Christensen-Dalsgaard, M.1    Gerdes, K.2
  • 39
    • 33846200333 scopus 로고    scopus 로고
    • Characterization of a higBA toxin-antitoxin locus in Vibrio cholerae
    • Budde PP, Davis BM, Yuan J, Waldor MK (2007) Characterization of a higBA toxin-antitoxin locus in Vibrio cholerae. J Bacteriol 189: 491-500.
    • (2007) J Bacteriol , vol.189 , pp. 491-500
    • Budde, P.P.1    Davis, B.M.2    Yuan, J.3    Waldor, M.K.4
  • 41
    • 0032464349 scopus 로고    scopus 로고
    • Analysis of zinc binding sites in protein crystal structures
    • Alberts IL, Nadassy K, Wodak SJ (1998) Analysis of zinc binding sites in protein crystal structures. Protein Sci 7: 1700-1716.
    • (1998) Protein Sci , vol.7 , pp. 1700-1716
    • Alberts, I.L.1    Nadassy, K.2    Wodak, S.J.3
  • 42
    • 0031446594 scopus 로고    scopus 로고
    • Classification of mononuclear zinc metal sites in protein structures
    • Karlin S, Zhu ZY (1997) Classification of mononuclear zinc metal sites in protein structures. Proc Natl Acad Sci U S A 94: 14231-14236.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 14231-14236
    • Karlin, S.1    Zhu, Z.Y.2
  • 43
    • 85142150362 scopus 로고    scopus 로고
    • Holm L, Kaariainen S, Rosenstrom P, Schenkel A (2008) Searching protein structure databases with DaliLite v.3. Bioinformatics 24: 2780-2781.
    • Holm L, Kaariainen S, Rosenstrom P, Schenkel A (2008) Searching protein structure databases with DaliLite v.3. Bioinformatics 24: 2780-2781.
  • 45
    • 67649794729 scopus 로고    scopus 로고
    • Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA interferase active site
    • Li GY, Zhang Y, Inouye M, Ikura M (2009) Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA interferase active site. J Biol Chem 284: 14628-14636.
    • (2009) J Biol Chem , vol.284 , pp. 14628-14636
    • Li, G.Y.1    Zhang, Y.2    Inouye, M.3    Ikura, M.4
  • 46
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 247: 536-540.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 47
    • 0141746380 scopus 로고    scopus 로고
    • Contribution of active site residues to the activity and thermal stability of ribonuclease Sa
    • Yakovlev GI, Mitkevich VA, Shaw KL, Trevino S, Newsom S, et al. (2003) Contribution of active site residues to the activity and thermal stability of ribonuclease Sa. Protein Sci 12: 2367-2373.
    • (2003) Protein Sci , vol.12 , pp. 2367-2373
    • Yakovlev, G.I.1    Mitkevich, V.A.2    Shaw, K.L.3    Trevino, S.4    Newsom, S.5
  • 48
    • 0027293405 scopus 로고
    • Complex of ribonuclease Sa with a cyclic nucleotide and a proposed model for the reaction intermediate
    • Sevcik J, Zegers I, Wyns L, Dauter Z, Wilson KS (1993) Complex of ribonuclease Sa with a cyclic nucleotide and a proposed model for the reaction intermediate. Eur J Biochem 216: 301-305.
    • (1993) Eur J Biochem , vol.216 , pp. 301-305
    • Sevcik, J.1    Zegers, I.2    Wyns, L.3    Dauter, Z.4    Wilson, K.S.5
  • 49
    • 53149133857 scopus 로고    scopus 로고
    • Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein
    • Kumar P, Issac B, Dodson EJ, Turkenburg JP, Mande SC (2008) Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein. J Mol Biol 383: 482-493.
    • (2008) J Mol Biol , vol.383 , pp. 482-493
    • Kumar, P.1    Issac, B.2    Dodson, E.J.3    Turkenburg, J.P.4    Mande, S.C.5
  • 50
    • 33750420023 scopus 로고    scopus 로고
    • The HicAB cassette, a putative novel, RNA-targeting toxin-antitoxin system in archaea and bacteria
    • Makarova KS, Grishin NV, Koonin EV (2006) The HicAB cassette, a putative novel, RNA-targeting toxin-antitoxin system in archaea and bacteria. Bioinformatics 22: 2581-2584.
    • (2006) Bioinformatics , vol.22 , pp. 2581-2584
    • Makarova, K.S.1    Grishin, N.V.2    Koonin, E.V.3
  • 51
    • 39749145842 scopus 로고    scopus 로고
    • P22 c2 repressor-operator complex: Mechanisms of direct and indirect readout
    • Watkins D, Hsiao C, Woods KK, Koudelka GB, Williams LD (2008) P22 c2 repressor-operator complex: mechanisms of direct and indirect readout. Biochemistry 47: 2325-2338.
    • (2008) Biochemistry , vol.47 , pp. 2325-2338
    • Watkins, D.1    Hsiao, C.2    Woods, K.K.3    Koudelka, G.B.4    Williams, L.D.5
  • 52
    • 0036136382 scopus 로고    scopus 로고
    • Directed evolution of toluene ortho-monooxygenase for enhanced 1-naphthol synthesis and chlorinated ethene degradation
    • Canada KA, Iwashita S, Shim H, Wood TK (2002) Directed evolution of toluene ortho-monooxygenase for enhanced 1-naphthol synthesis and chlorinated ethene degradation. J Bacteriol 184: 344-349.
    • (2002) J Bacteriol , vol.184 , pp. 344-349
    • Canada, K.A.1    Iwashita, S.2    Shim, H.3    Wood, T.K.4
  • 53
    • 0025968675 scopus 로고
    • Evaluation of Methods for Sampling, Recovery, and Enumeration of Bacteria Applied to the Phylloplane
    • Donegan K, Matyac C, Seidler R, Porteous A (1991) Evaluation of Methods for Sampling, Recovery, and Enumeration of Bacteria Applied to the Phylloplane. Appl Environ Microbiol 57: 51-56.
    • (1991) Appl Environ Microbiol , vol.57 , pp. 51-56
    • Donegan, K.1    Matyac, C.2    Seidler, R.3    Porteous, A.4
  • 54
    • 33751419975 scopus 로고    scopus 로고
    • Strategies to maximize heterologous protein expression in Escherichia coli with minimal cost
    • Peti W, Page R (2007) Strategies to maximize heterologous protein expression in Escherichia coli with minimal cost. Protein Expr Purif 51: 1-10.
    • (2007) Protein Expr Purif , vol.51 , pp. 1-10
    • Peti, W.1    Page, R.2
  • 55
    • 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. Macromolecular Crystallography Pt A 276: 307-326.
    • (1997) Macromolecular Crystallography Pt , vol.A 276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 57
  • 59
    • 0037441653 scopus 로고    scopus 로고
    • Lovell SC, Davis IW, Arendall WB 3rd, de Bakker PI, Word JM, et al. (2003) Structure validation by Calpha geometry: phi,psi and Cbeta deviation. Proteins 50: 437-450.
    • Lovell SC, Davis IW, Arendall WB 3rd, de Bakker PI, Word JM, et al. (2003) Structure validation by Calpha geometry: phi,psi and Cbeta deviation. Proteins 50: 437-450.
  • 60
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine AA, Richelle J, Wodak SJ (1999) SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr D Biol Crystallogr 55: 191-205.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.