메뉴 건너뛰기




Volumn 4, Issue 1, 2009, Pages

The contribution of polystyrene nanospheres towards the crystallization of proteins

Author keywords

[No Author keywords available]

Indexed keywords

HYDROPHOBIN; HYDROPHOBIN 1; HYDROPHOBIN 2; IMMUNOGLOBULIN F(AB) FRAGMENT; LACCASE; LYSOZYME; METHYLTRANSFERASE; NANOSPHERE; POLYSTYRENE; PROTEIN; SARCOSINE DIMETHYLGLYCINE N METHYLTRANSFERASE; TESTOSTERONE F(AB) FRAGMENT 5F2 ANTIBODY; UNCLASSIFIED DRUG; XYLAN ENDO 1,3 BETA XYLOSIDASE; XYLOSE ISOMERASE; POLYSTYRENE DERIVATIVE;

EID: 58449091226     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0004198     Document Type: Article
Times cited : (23)

References (27)
  • 1
    • 0037391080 scopus 로고    scopus 로고
    • Seeds to crystals
    • Bergfors T (2003) Seeds to crystals. J Struct Biol 142: 66-76.
    • (2003) J Struct Biol , vol.142 , pp. 66-76
    • Bergfors, T.1
  • 2
    • 7444264009 scopus 로고    scopus 로고
    • Microseed matrix screening to improve crystals of yeast cytosine deaminase
    • Ireton GC, Stoddard BL (2004) Microseed matrix screening to improve crystals of yeast cytosine deaminase. Acta Crystallogr Sect D Biol Crystallogr 60: 601-605.
    • (2004) Acta Crystallogr Sect D Biol Crystallogr , vol.60 , pp. 601-605
    • Ireton, G.C.1    Stoddard, B.L.2
  • 3
    • 33947537616 scopus 로고    scopus 로고
    • An automated microseed matrix-screening method for protein crystallization
    • D'Arcy A, Villard F, Marsh M (2007) An automated microseed matrix-screening method for protein crystallization. Acta Crystallogr Sect D Biol Crystallogr 63: 550-554.
    • (2007) Acta Crystallogr Sect D Biol Crystallogr , vol.63 , pp. 550-554
    • D'Arcy, A.1    Villard, F.2    Marsh, M.3
  • 4
    • 0038116273 scopus 로고    scopus 로고
    • Using natural seeding material to generate nucleation in protein crystallization experiments
    • D'Arcy A, Sweeney AM, Haber A (2003) Using natural seeding material to generate nucleation in protein crystallization experiments. Acta Crystallogr Sect D Biol Crystallogr 59: 1343-1346.
    • (2003) Acta Crystallogr Sect D Biol Crystallogr , vol.59 , pp. 1343-1346
    • D'Arcy, A.1    Sweeney, A.M.2    Haber, A.3
  • 7
    • 0000909155 scopus 로고
    • Heterogeneous and epitaxial nucleation of protein crystals on mineral surfaces
    • McPherson A, Shlichta P (1988) Heterogeneous and epitaxial nucleation of protein crystals on mineral surfaces. Science 239: 385-387.
    • (1988) Science , vol.239 , pp. 385-387
    • McPherson, A.1    Shlichta, P.2
  • 8
    • 31444449113 scopus 로고    scopus 로고
    • Experiment and theory for heterogeneous nucleation of protein crystals in a porous medium
    • Chayen NE, Saridakis E, Sear RP (2006) Experiment and theory for heterogeneous nucleation of protein crystals in a porous medium. Proc Natl Acad Sci U S A 103: 597-601.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 597-601
    • Chayen, N.E.1    Saridakis, E.2    Sear, R.P.3
  • 10
    • 0035502184 scopus 로고    scopus 로고
    • Accelerated protein crystal growth by protein thin film template
    • Pechkova E, Nicolini C (2001) Accelerated protein crystal growth by protein thin film template. J Cryst Growth 231: 599-602.
    • (2001) J Cryst Growth , vol.231 , pp. 599-602
    • Pechkova, E.1    Nicolini, C.2
  • 11
    • 1242338109 scopus 로고    scopus 로고
    • Protein nanocrystallography: A new approach to structural proteomics
    • Pechkova E, Nicolini C (2004) Protein nanocrystallography: a new approach to structural proteomics. Trends Biotechnol 22: 117-122.
    • (2004) Trends Biotechnol , vol.22 , pp. 117-122
    • Pechkova, E.1    Nicolini, C.2
  • 12
    • 23844435319 scopus 로고    scopus 로고
    • Investigating crystal-growth mechanisms with and without LB template: Protein transfer from LB to crystal
    • Pechkova E, Fiordoro S, Fontani D, Nicolini C (2005) Investigating crystal-growth mechanisms with and without LB template: protein transfer from LB to crystal. Acta Crystallogr Sect D Biol Crystallogr 61: 809-812.
    • (2005) Acta Crystallogr Sect D Biol Crystallogr , vol.61 , pp. 809-812
    • Pechkova, E.1    Fiordoro, S.2    Fontani, D.3    Nicolini, C.4
  • 14
    • 0347683444 scopus 로고    scopus 로고
    • Atomic resolution structure of the HFBII hydrophobin: A self-assembling amphiphile
    • Hakanpää J, Paananen A, Askolin S Nakari-Setälä T, Parkkinen T, et al. (2004) Atomic resolution structure of the HFBII hydrophobin: a self-assembling amphiphile. J Biol Chem 279: 534-539.
    • (2004) J Biol Chem , vol.279 , pp. 534-539
    • Hakanpää, J.1    Paananen, A.2    Askolin, S.3    Nakari-Setälä, T.4    Parkkinen, T.5
  • 15
    • 35348966768 scopus 로고    scopus 로고
    • Crystal structures of hydrophobin HFBII in the presence of detergent implicate the formation of fibrils and monolayer films
    • Kallio JM, Linder MB, Rouvinen J (2007) Crystal structures of hydrophobin HFBII in the presence of detergent implicate the formation of fibrils and monolayer films. J Biol Chem 282: 28733-28739.
    • (2007) J Biol Chem , vol.282 , pp. 28733-28739
    • Kallio, J.M.1    Linder, M.B.2    Rouvinen, J.3
  • 16
    • 33746064591 scopus 로고    scopus 로고
    • Two crystal structures of Trichoderma reesei hydrophobin HFBI - a structure of a protein amphiphile with and without detergent
    • Hakanpää J, Szilvay GR, Kaljunen H, Maksimainen M, Linder M, et al. (2006) Two crystal structures of Trichoderma reesei hydrophobin HFBI - a structure of a protein amphiphile with and without detergent. Protein Sci 15: 2129-2140.
    • (2006) Protein Sci , vol.15 , pp. 2129-2140
    • Hakanpää, J.1    Szilvay, G.R.2    Kaljunen, H.3    Maksimainen, M.4    Linder, M.5
  • 17
    • 41649119963 scopus 로고    scopus 로고
    • A near atomic resolution structure of a Melanocarpus albomyces laccase
    • Hakulinen N, Andberg M, Kallio J, Koivula A, Kruus K, et al. (2008) A near atomic resolution structure of a Melanocarpus albomyces laccase. J Struct Biol 162: 29-39.
    • (2008) J Struct Biol , vol.162 , pp. 29-39
    • Hakulinen, N.1    Andberg, M.2    Kallio, J.3    Koivula, A.4    Kruus, K.5
  • 18
    • 33750052272 scopus 로고    scopus 로고
    • A crystallographic and spectroscopic study on the effect of X-ray radiation on the crystal structure of Melanocarpus albomyces laccase
    • Hakulinen N, Kruus K, Koivula A, Rouvinen J (2006) A crystallographic and spectroscopic study on the effect of X-ray radiation on the crystal structure of Melanocarpus albomyces laccase. Biochim Biophys Research Comm 350: 929-934.
    • (2006) Biochim Biophys Research Comm , vol.350 , pp. 929-934
    • Hakulinen, N.1    Kruus, K.2    Koivula, A.3    Rouvinen, J.4
  • 19
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW (1968) Solvent content of protein crystals. J Mol Biol 33: 491-497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 20
    • 0002737621 scopus 로고
    • Isolation of lysozvme from egg white
    • Alderton G, Ward W, Febold H (1945) Isolation of lysozvme from egg white. J Biol Chem 157: 43-58.
    • (1945) J Biol Chem , vol.157 , pp. 43-58
    • Alderton, G.1    Ward, W.2    Febold, H.3
  • 21
    • 0028338985 scopus 로고
    • Three dimensional structure of the endo-1,4-beta-xylanase II from Trichoderma reesei: Two conformational states in the active site
    • Törrönen A, Harkki A, Rouvinen J (1994) Three dimensional structure of the endo-1,4-beta-xylanase II from Trichoderma reesei: two conformational states in the active site. EMBO J 13: 2493-2501.
    • (1994) EMBO J , vol.13 , pp. 2493-2501
    • Törrönen, A.1    Harkki, A.2    Rouvinen, J.3
  • 22
    • 0001304049 scopus 로고
    • X-ray analysis of D-xylose isomerase at 1.9 Å: Native enzyme in complex with substrate and with a mechanism-designed inactivator
    • Carrell HL, Glusker JP, Burger V, Manfre F, Tritsch D, et al. (1989) X-ray analysis of D-xylose isomerase at 1.9 Å: native enzyme in complex with substrate and with a mechanism-designed inactivator. Proc Natl Acad Sci U S A 86: 4440-4444.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 4440-4444
    • Carrell, H.L.1    Glusker, J.P.2    Burger, V.3    Manfre, F.4    Tritsch, D.5
  • 23
    • 0030053545 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of the Trichoderma reesei hvdrophobin HFBI
    • Nakari-Setälä T, Aro N, Kalkkinen N, Alatalo E, Penttilä M (1996) Genetic and biochemical characterization of the Trichoderma reesei hvdrophobin HFBI. Eur J Biochem 235: 248-255.
    • (1996) Eur J Biochem , vol.235 , pp. 248-255
    • Nakari-Setälä, T.1    Aro, N.2    Kalkkinen, N.3    Alatalo, E.4    Penttilä, M.5
  • 24
    • 0030886123 scopus 로고    scopus 로고
    • Differential expression of the vegetative and spore-bound hydrophobins of Trichoderma reesei. Cloning and characterization of the hfb2 gene
    • Nakari-Setälä T, Aro N, Ilmén M, Muños G, Kalkkinen N, et al. (1997) Differential expression of the vegetative and spore-bound hydrophobins of Trichoderma reesei. Cloning and characterization of the hfb2 gene. Eur J Biochem 248: 415-423.
    • (1997) Eur J Biochem , vol.248 , pp. 415-423
    • Nakari-Setälä, T.1    Aro, N.2    Ilmén, M.3    Muños, G.4    Kalkkinen, N.5
  • 25
    • 4844228512 scopus 로고    scopus 로고
    • Expression of Melanocarpus albomyces laccase in Trichoderma reesei and charachterization of the purified enzyme
    • Kiiskinen LL, Kruus K, Bailey M, Ylösmäki E, Siika-Aho M, et al. (2004) Expression of Melanocarpus albomyces laccase in Trichoderma reesei and charachterization of the purified enzyme. Microbiology 150: 3065-3074.
    • (2004) Microbiology , vol.150 , pp. 3065-3074
    • Kiiskinen, L.L.1    Kruus, K.2    Bailey, M.3    Ylösmäki, E.4    Siika-Aho, M.5
  • 26
    • 0035344465 scopus 로고    scopus 로고
    • Charachterization of glycine sarcosine N-methyltransferase and sarcosince dimethylglycine N-methyltransferase
    • Nyyssölä A, Reinikainen T, Leisola M (2001) Charachterization of glycine sarcosine N-methyltransferase and sarcosince dimethylglycine N-methyltransferase. Appl Environ Microbiol 67: 2044-2050.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 2044-2050
    • Nyyssölä, A.1    Reinikainen, T.2    Leisola, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.