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Volumn 16, Issue 11, 2007, Pages 2542-2551

Polymer-driven crystallization

Author keywords

Crystallization module; Membrane protein; Protein crystallization; Protein polymer; Sterile alpha motif domains

Indexed keywords

HYBRID PROTEIN; MEMBRANE PROTEIN; POLYMER; TRANSCRIPTION FACTOR ETV6;

EID: 35649018258     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.073074207     Document Type: Article
Times cited : (32)

References (64)
  • 2
    • 0033517711 scopus 로고    scopus 로고
    • The leukemia-associated gene TEL encodes a transcription repressor which associates with SMRT and mSin3A
    • Chakrabarti, S.R. and Nucifora, G. 1999. The leukemia-associated gene TEL encodes a transcription repressor which associates with SMRT and mSin3A. Biochem. Biophys. Res. Commun. 264: 871-877.
    • (1999) Biochem. Biophys. Res. Commun , vol.264 , pp. 871-877
    • Chakrabarti, S.R.1    Nucifora, G.2
  • 3
    • 8844222708 scopus 로고    scopus 로고
    • TargetDB: A target registration database for structural genomics projects
    • Chen, L., Oughtred, R., Berman, H.M., and Westbrook, J. 2004. TargetDB: A target registration database for structural genomics projects. Bioinformatics 20: 2860-2862.
    • (2004) Bioinformatics , vol.20 , pp. 2860-2862
    • Chen, L.1    Oughtred, R.2    Berman, H.M.3    Westbrook, J.4
  • 4
    • 0016396449 scopus 로고
    • Crystallisation of a modified fibrinogen
    • Cohen, C. and Tooney, N.M. 1974. Crystallisation of a modified fibrinogen. Nature 251: 659-660.
    • (1974) Nature , vol.251 , pp. 659-660
    • Cohen, C.1    Tooney, N.M.2
  • 6
    • 0001434101 scopus 로고
    • Crystallizing proteins - A rational approach?
    • D'Arcy, A. 1994. Crystallizing proteins - A rational approach? Acta Crystallogr. D Biol. Crystallogr. 50: 469-471.
    • (1994) Acta Crystallogr. D Biol. Crystallogr , vol.50 , pp. 469-471
    • D'Arcy, A.1
  • 7
    • 0033198986 scopus 로고    scopus 로고
    • Crystal engineering: A case study using the 24 kDa fragment of the DNA gyrase B subunit from Escherichia coli
    • D'Arcy, A., Stihle, M., Kostrewa, D., and Dale, G. 1999. Crystal engineering: A case study using the 24 kDa fragment of the DNA gyrase B subunit from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 55: 1623-1625.
    • (1999) Acta Crystallogr. D Biol. Crystallogr , vol.55 , pp. 1623-1625
    • D'Arcy, A.1    Stihle, M.2    Kostrewa, D.3    Dale, G.4
  • 8
    • 0037391084 scopus 로고    scopus 로고
    • The protein as a variable in protein crystallization
    • Dale, G.E., Oefner, C., and D'Arcy, A. 2003. The protein as a variable in protein crystallization. J. Struct. Biol. 142: 88-97.
    • (2003) J. Struct. Biol , vol.142 , pp. 88-97
    • Dale, G.E.1    Oefner, C.2    D'Arcy, A.3
  • 9
    • 33751436135 scopus 로고    scopus 로고
    • Solution structure and dynamics of the N-terminal cytosolic domain of rhomboid intramembrane protease from Pseudomonas aeruginosa: Insights into a functional role in intramembrane proteolysis
    • Del Rio, A., Dutta, K., Chavez, J., Ubarretxena-Belandia, I., and Ghose, R. 2007. Solution structure and dynamics of the N-terminal cytosolic domain of rhomboid intramembrane protease from Pseudomonas aeruginosa: Insights into a functional role in intramembrane proteolysis. J. Mol. Biol. 365: 109-122.
    • (2007) J. Mol. Biol , vol.365 , pp. 109-122
    • Del Rio, A.1    Dutta, K.2    Chavez, J.3    Ubarretxena-Belandia, I.4    Ghose, R.5
  • 10
    • 1842555070 scopus 로고    scopus 로고
    • Rational protein crystallization by mutational surface engineering
    • Derewenda, Z.S. 2004a. Rational protein crystallization by mutational surface engineering. Structure 12: 529-535.
    • (2004) Structure , vol.12 , pp. 529-535
    • Derewenda, Z.S.1
  • 11
    • 4344698577 scopus 로고    scopus 로고
    • The use of recombinant methods and molecular engineering in protein crystallization
    • Derewenda, Z.S. 2004b. The use of recombinant methods and molecular engineering in protein crystallization. Methods 34: 354-363.
    • (2004) Methods , vol.34 , pp. 354-363
    • Derewenda, Z.S.1
  • 13
    • 0028135357 scopus 로고
    • Three-dimensional structure of the platelet integrin recognition segment of the fibrinogen γ chain obtained by carrier protein-driven crystallization
    • Donahue, J.P., Patel, H., Anderson, W.F., and Hawiger, J. 1994. Three-dimensional structure of the platelet integrin recognition segment of the fibrinogen γ chain obtained by carrier protein-driven crystallization. Proc. Natl. Acad. Sci. 91: 12178-12182.
    • (1994) Proc. Natl. Acad. Sci , vol.91 , pp. 12178-12182
    • Donahue, J.P.1    Patel, H.2    Anderson, W.F.3    Hawiger, J.4
  • 14
    • 13244281317 scopus 로고    scopus 로고
    • COOT: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. 2004. COOT: Model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60: 2126-2132.
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 15
    • 0025047629 scopus 로고
    • A mutant T4 lysozyme displays five different conformations
    • Faber, H.R. and Matthews, B.W. 1990. A mutant T4 lysozyme displays five different conformations. Nature 348: 263-266.
    • (1990) Nature , vol.348 , pp. 263-266
    • Faber, H.R.1    Matthews, B.W.2
  • 16
    • 4344714933 scopus 로고    scopus 로고
    • Synthetic antibodies from a four-amino-acid code: A dominant role for tyrosine in antigen recognition
    • Fellouse, F.A., Wiesmann, C., and Sidhu, S.S. 2004. Synthetic antibodies from a four-amino-acid code: A dominant role for tyrosine in antigen recognition. Proc. Natl. Acad. Sci. 101: 12467-12472.
    • (2004) Proc. Natl. Acad. Sci , vol.101 , pp. 12467-12472
    • Fellouse, F.A.1    Wiesmann, C.2    Sidhu, S.S.3
  • 17
    • 2442564417 scopus 로고    scopus 로고
    • The Drosophila Polycomb group gene Sex combs extra encodes the ortholog of mammalian Ring1 proteins
    • Gorfinkiel, N., Fanti, L., Melgar, T., Garcia, E., Pimpinelli, S., Guerrero, I., and Vidal, M. 2004. The Drosophila Polycomb group gene Sex combs extra encodes the ortholog of mammalian Ring1 proteins. Mech. Dev. 121: 449-462.
    • (2004) Mech. Dev , vol.121 , pp. 449-462
    • Gorfinkiel, N.1    Fanti, L.2    Melgar, T.3    Garcia, E.4    Pimpinelli, S.5    Guerrero, I.6    Vidal, M.7
  • 18
    • 0028334576 scopus 로고
    • Crystal structures of Y41H and Y41F mutants of gene V protein from Ff phage suggest possible protein-protein interactions in the GVP-ssDNA complex
    • Guan, Y., Zhang, H., Konings, R.N., Hilbers, C.W., Terwilliger, T.C., and Wang, A.H. 1994. Crystal structures of Y41H and Y41F mutants of gene V protein from Ff phage suggest possible protein-protein interactions in the GVP-ssDNA complex. Biochemistry 33: 7768-7778.
    • (1994) Biochemistry , vol.33 , pp. 7768-7778
    • Guan, Y.1    Zhang, H.2    Konings, R.N.3    Hilbers, C.W.4    Terwilliger, T.C.5    Wang, A.H.6
  • 19
    • 0036084604 scopus 로고    scopus 로고
    • Crystal structures of free, IMP-, and GMP-bound Escherichia coli hypoxanthine phosphoribosyltransferase
    • Guddat, L.W., Vos, S., Martin, J.L., Keough, D.T., and de Jersey, J. 2002. Crystal structures of free, IMP-, and GMP-bound Escherichia coli hypoxanthine phosphoribosyltransferase. Protein Sci. 11: 1626-1638.
    • (2002) Protein Sci , vol.11 , pp. 1626-1638
    • Guddat, L.W.1    Vos, S.2    Martin, J.L.3    Keough, D.T.4    de Jersey, J.5
  • 20
    • 0028158008 scopus 로고
    • Rapid crystallization of T4 lysozyme by intermolecular disulfide cross-linking
    • Heinz, D.W. and Matthews, B.W. 1994. Rapid crystallization of T4 lysozyme by intermolecular disulfide cross-linking. Protein Eng. 7: 301-307.
    • (1994) Protein Eng , vol.7 , pp. 301-307
    • Heinz, D.W.1    Matthews, B.W.2
  • 21
    • 0029990345 scopus 로고    scopus 로고
    • A flexible loop at the dimer interface is a part of the active site of the adjacent monomer of Escherichia coli orotate phosphoribosyltransferase
    • Henriksen, A., Aghajari, N., Jensen, K.F., and Gajhede, M. 1996. A flexible loop at the dimer interface is a part of the active site of the adjacent monomer of Escherichia coli orotate phosphoribosyltransferase. Biochemistry 35: 3803-3809.
    • (1996) Biochemistry , vol.35 , pp. 3803-3809
    • Henriksen, A.1    Aghajari, N.2    Jensen, K.F.3    Gajhede, M.4
  • 22
    • 32944467057 scopus 로고    scopus 로고
    • Post-crystallization treatments for improving diffraction quality of protein crystals
    • Heras, B. and Martin, J.L. 2005. Post-crystallization treatments for improving diffraction quality of protein crystals. Acta Crystallogr. D Biol. Crystallogr. 61: 1173-1180.
    • (2005) Acta Crystallogr. D Biol. Crystallogr , vol.61 , pp. 1173-1180
    • Heras, B.1    Martin, J.L.2
  • 23
    • 0036667741 scopus 로고    scopus 로고
    • Crystallisation of membrane proteins mediated by antibody fragments
    • Hunte, C. and Michel, H. 2002. Crystallisation of membrane proteins mediated by antibody fragments. Curr. Opin. Struct. Biol. 12: 503-508.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 503-508
    • Hunte, C.1    Michel, H.2
  • 24
    • 0034660152 scopus 로고    scopus 로고
    • (1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment
    • (1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment. Structure 8: 669-684.
    • (2000) Structure , vol.8 , pp. 669-684
    • Hunte, C.1    Koepke, J.2    Lange, C.3    Rossmanith, T.4    Michel, H.5
  • 25
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata, S., Ostermeier, C., Ludwig, B., and Michel, H. 1995. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376: 660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 30
    • 0035421962 scopus 로고    scopus 로고
    • Polymerization of the SAM domain of TEL in leukemogenesis and transcriptional repression
    • Kim, C.A., Phillips, M.L., Kim, W., Gingery, M., Tran, H.H., Robinson, M.A., Faham, S., and Bowie, J.U. 2001. Polymerization of the SAM domain of TEL in leukemogenesis and transcriptional repression. EMBO J. 20: 4173-4182.
    • (2001) EMBO J , vol.20 , pp. 4173-4182
    • Kim, C.A.1    Phillips, M.L.2    Kim, W.3    Gingery, M.4    Tran, H.H.5    Robinson, M.A.6    Faham, S.7    Bowie, J.U.8
  • 31
    • 0028798287 scopus 로고
    • Engineered Fv fragments as a tool for the one-step purification of integral multisubunit membrane protein complexes
    • Kleymann, G., Ostermeier, C., Ludwig, B., Skerra, A., and Michel, H. 1995. Engineered Fv fragments as a tool for the one-step purification of integral multisubunit membrane protein complexes. Biotechnology (N.Y.) 13: 155-160.
    • (1995) Biotechnology (N.Y.) , vol.13 , pp. 155-160
    • Kleymann, G.1    Ostermeier, C.2    Ludwig, B.3    Skerra, A.4    Michel, H.5
  • 32
    • 34249852867 scopus 로고    scopus 로고
    • High-affinity single-domain binding proteins with a binary-code interface
    • Koide, A., Gilbreth, R.N., Esaki, K., Tereshko, V., and Koide, S. 2007. High-affinity single-domain binding proteins with a binary-code interface. Proc. Natl. Acad. Sci. 104: 6632-6637.
    • (2007) Proc. Natl. Acad. Sci , vol.104 , pp. 6632-6637
    • Koide, A.1    Gilbreth, R.N.2    Esaki, K.3    Tereshko, V.4    Koide, S.5
  • 33
    • 0030861664 scopus 로고    scopus 로고
    • Use of a fusion protein to obtain crystals suitable for X-ray analysis: Crystallization of a GST-fused protein containing the DNA-binding domain of DNA replication-related element-binding factor, DREF
    • Kuge, M., Fujii, Y., Shimizu, T., Hirose, F., Matsukage, A., and Hakoshima, T. 1997. Use of a fusion protein to obtain crystals suitable for X-ray analysis: Crystallization of a GST-fused protein containing the DNA-binding domain of DNA replication-related element-binding factor, DREF. Protein Sci. 6: 1783-1786.
    • (1997) Protein Sci , vol.6 , pp. 1783-1786
    • Kuge, M.1    Fujii, Y.2    Shimizu, T.3    Hirose, F.4    Matsukage, A.5    Hakoshima, T.6
  • 34
    • 0036300662 scopus 로고    scopus 로고
    • Accurate computer-based design of a new backbone conformation in the second turn of protein L
    • Kuhlman, B., O'Neill, J.W., Kim, D.E., Zhang, K.Y., and Baker, D. 2002. Accurate computer-based design of a new backbone conformation in the second turn of protein L. J. Mol. Biol. 315: 471-477.
    • (2002) J. Mol. Biol , vol.315 , pp. 471-477
    • Kuhlman, B.1    O'Neill, J.W.2    Kim, D.E.3    Zhang, K.Y.4    Baker, D.5
  • 35
    • 0033548254 scopus 로고    scopus 로고
    • Probability analysis of variational crystallization and its application to gp120, the exterior envelope glycoprotein of type 1 human immunodeficiency virus (HIV-1)
    • Kwong, P.D., Wyatt, R., Desjardins, E., Robinson, J., Culp, J.S., Hellmig, B.D., Sweet, R.W., Sodroski, J., and Hendrickson, W.A. 1999. Probability analysis of variational crystallization and its application to gp120, the exterior envelope glycoprotein of type 1 human immunodeficiency virus (HIV-1). J. Biol. Chem. 274: 4115-4123.
    • (1999) J. Biol. Chem , vol.274 , pp. 4115-4123
    • Kwong, P.D.1    Wyatt, R.2    Desjardins, E.3    Robinson, J.4    Culp, J.S.5    Hellmig, B.D.6    Sweet, R.W.7    Sodroski, J.8    Hendrickson, W.A.9
  • 39
    • 0037394492 scopus 로고    scopus 로고
    • A deliberate approach to screening for initial crystallization conditions of biological macromolecules
    • Luft, J.R., Collins, R.J., Fehrman, N.A., Lauricella, A.M., Veatch, C.K., and DeTitta, G.T. 2003. A deliberate approach to screening for initial crystallization conditions of biological macromolecules. J. Struct. Biol. 142: 170-179.
    • (2003) J. Struct. Biol , vol.142 , pp. 170-179
    • Luft, J.R.1    Collins, R.J.2    Fehrman, N.A.3    Lauricella, A.M.4    Veatch, C.K.5    DeTitta, G.T.6
  • 41
    • 0028931691 scopus 로고
    • Crystal structures of a schistosomal drug and vaccine target: Glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel
    • McTigue, M.A., Williams, D.R., and Tainer, J.A. 1995. Crystal structures of a schistosomal drug and vaccine target: Glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel. J. Mol. Biol. 246: 21-27.
    • (1995) J. Mol. Biol , vol.246 , pp. 21-27
    • McTigue, M.A.1    Williams, D.R.2    Tainer, J.A.3
  • 42
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: The integration of data reduction and structure solution - from diffraction images to an initial model in minutes
    • Minor, W., Cymborowski, M., Otwinowski, Z., and Chruszcz, M. 2006. HKL-3000: The integration of data reduction and structure solution - from diffraction images to an initial model in minutes. Acta Crystallogr. D Biol. Crystallogr. 62: 859-866.
    • (2006) Acta Crystallogr. D Biol. Crystallogr , vol.62 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 43
    • 0036892410 scopus 로고    scopus 로고
    • Crystal structures and increased stabilization of the protein G variants with switched folding pathways NuG1 and NuG2
    • Nauli, S., Kuhlman, B., Le Trong, I., Stenkamp, R.E., Teller, D., and Baker, D. 2002. Crystal structures and increased stabilization of the protein G variants with switched folding pathways NuG1 and NuG2. Protein Sci. 11: 2924-2931.
    • (2002) Protein Sci , vol.11 , pp. 2924-2931
    • Nauli, S.1    Kuhlman, B.2    Le Trong, I.3    Stenkamp, R.E.4    Teller, D.5    Baker, D.6
  • 44
    • 33745969466 scopus 로고    scopus 로고
    • A simple strategy towards membrane protein purification and crystallization
    • Niegowski, D., Hedren, M., Nordlund, P., and Eshaghi, S. 2006. A simple strategy towards membrane protein purification and crystallization. Int. J. Biol. Macromol. 39: 83-87.
    • (2006) Int. J. Biol. Macromol , vol.39 , pp. 83-87
    • Niegowski, D.1    Hedren, M.2    Nordlund, P.3    Eshaghi, S.4
  • 46
    • 0028991525 scopus 로고
    • Fv fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase
    • Ostermeier, C., Iwata, S., Ludwig, B., and Michel, H. 1995. Fv fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase. Nat. Struct. Biol. 2: 842-846.
    • (1995) Nat. Struct. Biol , vol.2 , pp. 842-846
    • Ostermeier, C.1    Iwata, S.2    Ludwig, B.3    Michel, H.4
  • 47
    • 0037305856 scopus 로고    scopus 로고
    • Crystal structure of a trimeric form of dephosphocoenzyme A kinase from Escherichia coli
    • O'Toole, N., Barbosa, J.A., Li, Y., Hung, L.W., Matte, A., and Cygler, M. 2003. Crystal structure of a trimeric form of dephosphocoenzyme A kinase from Escherichia coli. Protein Sci. 12: 327-336.
    • (2003) Protein Sci , vol.12 , pp. 327-336
    • O'Toole, N.1    Barbosa, J.A.2    Li, Y.3    Hung, L.W.4    Matte, A.5    Cygler, M.6
  • 48
    • 11244313165 scopus 로고    scopus 로고
    • Developmentally regulated alterations in Polycomb repressive complex 1 proteins on the inactive X chromosome
    • Plath, K., Talbot, D., Hamer, K.M., Otte, A.P., Yang, T.P., Jaenisch, R., and Panning, B. 2004. Developmentally regulated alterations in Polycomb repressive complex 1 proteins on the inactive X chromosome. J. Cell Biol. 167: 1025-1035.
    • (2004) J. Cell Biol , vol.167 , pp. 1025-1035
    • Plath, K.1    Talbot, D.2    Hamer, K.M.3    Otte, A.P.4    Yang, T.P.5    Jaenisch, R.6    Panning, B.7
  • 52
    • 0032927872 scopus 로고    scopus 로고
    • RING1 interacts with multiple Polycomb-group proteins and displays tumorigenic activity
    • Satijn, D.P. and Otte, A.P. 1999. RING1 interacts with multiple Polycomb-group proteins and displays tumorigenic activity. Mol. Cell. Biol. 19: 57-68.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 57-68
    • Satijn, D.P.1    Otte, A.P.2
  • 53
    • 1842364897 scopus 로고    scopus 로고
    • Ring1A is a transcriptional repressor that interacts with the Polycomb-M33 protein and is expressed at rhombomere boundaries in the mouse hindbrain
    • Schoorlemmer, J., Marcos-Gutierrez, C., Were, F., Martinez, R., Garcia, E., Satijn, D.P., Otte, A.P., and Vidal, M. 1997. Ring1A is a transcriptional repressor that interacts with the Polycomb-M33 protein and is expressed at rhombomere boundaries in the mouse hindbrain. EMBO J. 16: 5930-5942.
    • (1997) EMBO J , vol.16 , pp. 5930-5942
    • Schoorlemmer, J.1    Marcos-Gutierrez, C.2    Were, F.3    Martinez, R.4    Garcia, E.5    Satijn, D.P.6    Otte, A.P.7    Vidal, M.8
  • 54
    • 0035501932 scopus 로고    scopus 로고
    • Efficiency analysis of sampling protocols used in protein crystallization screening
    • Segelke, B.W. 2001. Efficiency analysis of sampling protocols used in protein crystallization screening. J. Cryst. Growth 232: 553-562.
    • (2001) J. Cryst. Growth , vol.232 , pp. 553-562
    • Segelke, B.W.1
  • 57
    • 0031836054 scopus 로고    scopus 로고
    • A thioredoxin fusion protein of VanH, a D-lactate dehydrogenase from Enterococcus faecium: Cloning, expression, purification, kinetic analysis, and crystallization
    • Stoll, V.S., Manohar, A.V., Gillon, W., MacFarlane, E.L., Hynes, R.C., and Pai, E.F. 1998. A thioredoxin fusion protein of VanH, a D-lactate dehydrogenase from Enterococcus faecium: Cloning, expression, purification, kinetic analysis, and crystallization. Protein Sci. 7: 1147-1155.
    • (1998) Protein Sci , vol.7 , pp. 1147-1155
    • Stoll, V.S.1    Manohar, A.V.2    Gillon, W.3    MacFarlane, E.L.4    Hynes, R.C.5    Pai, E.F.6
  • 58
    • 0015494742 scopus 로고
    • Microcrystals of a modified fibrinogen
    • Tooney, N.M. and Cohen, C. 1972. Microcrystals of a modified fibrinogen. Nature 237: 23-25.
    • (1972) Nature , vol.237 , pp. 23-25
    • Tooney, N.M.1    Cohen, C.2
  • 59
    • 33751246749 scopus 로고    scopus 로고
    • Rhomboid proteins: Conserved membrane proteases with divergent biological functions
    • Urban, S. 2006. Rhomboid proteins: Conserved membrane proteases with divergent biological functions. Genes & Dev. 20: 3054-3068.
    • (2006) Genes & Dev , vol.20 , pp. 3054-3068
    • Urban, S.1
  • 60
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin, E. and von Heijne, G. 1998. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 7: 1029-1038.
    • (1998) Protein Sci , vol.7 , pp. 1029-1038
    • Wallin, E.1    von Heijne, G.2
  • 61
    • 0033458848 scopus 로고    scopus 로고
    • Structure of the fibrinogen γ-chain integrin binding and factor XIIIa cross-linking sites obtained through carrier protein driven crystallization
    • Ware, S., Donahue, J.P., Hawiger, J., and Anderson, W.F. 1999. Structure of the fibrinogen γ-chain integrin binding and factor XIIIa cross-linking sites obtained through carrier protein driven crystallization. Protein Sci. 8: 2663-2671.
    • (1999) Protein Sci , vol.8 , pp. 2663-2671
    • Ware, S.1    Donahue, J.P.2    Hawiger, J.3    Anderson, W.F.4
  • 62
    • 0035960880 scopus 로고    scopus 로고
    • Structural analysis of regulatory protein domains using GST-fusion proteins
    • Zhan, Y., Song, X., and Zhou, G.W. 2001. Structural analysis of regulatory protein domains using GST-fusion proteins. Gene 281: 1-9.
    • (2001) Gene , vol.281 , pp. 1-9
    • Zhan, Y.1    Song, X.2    Zhou, G.W.3


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