메뉴 건너뛰기




Volumn 16, Issue 7, 2007, Pages 1422-1428

A high-throughput method for membrane protein solubility screening: The ultracentrifugation dispersity sedimentation assay

Author keywords

Aggregation; Detergent; High throughput; Membrane proteins; Monodispersity; Stability; Ultracentrifugation

Indexed keywords

BUFFER; DETERGENT; MEMBRANE PROTEIN;

EID: 34250833480     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.072759907     Document Type: Article
Times cited : (57)

References (25)
  • 2
    • 33751293464 scopus 로고    scopus 로고
    • Solubilization and purification of membrane proteins
    • ed. K.H. Lundstrom, pp, Taylor and Francis, New York
    • Byrne, B. and Jormakka, M. 2006. Solubilization and purification of membrane proteins. In Structural genomics on membrane proteins (ed. K.H. Lundstrom), pp. 179-198. Taylor and Francis, New York.
    • (2006) Structural genomics on membrane proteins , pp. 179-198
    • Byrne, B.1    Jormakka, M.2
  • 3
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • Chang, G., Spencer, R.H., Lee, A.T., Barclay, M.T., and Rees, D.C. 1998. Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel. Science 282: 2220-2226.
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 4
    • 33646147814 scopus 로고    scopus 로고
    • Expression, purification, and characterization of Thermotoga maritima membrane proteins for structure determination
    • Columbus, L., Lipfert, J., Klock, H., Millett, I., Doniach, S., and Lesley, S.A. 2006. Expression, purification, and characterization of Thermotoga maritima membrane proteins for structure determination. Protein Sci. 15: 961-975.
    • (2006) Protein Sci , vol.15 , pp. 961-975
    • Columbus, L.1    Lipfert, J.2    Klock, H.3    Millett, I.4    Doniach, S.5    Lesley, S.A.6
  • 5
    • 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
  • 6
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson, R.J. and Locher, K.P. 2006. Structure of a bacterial multidrug ABC transporter. Nature 443: 180-185.
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 7
    • 33645454462 scopus 로고    scopus 로고
    • Optimization of membrane protein overexpression and purification using GFP fusions
    • Drew, D., Lerch, M., Kunji, E., Slotboom, D.J., and de Gier, J.W. 2006. Optimization of membrane protein overexpression and purification using GFP fusions. Nat. Methods 3: 303-313.
    • (2006) Nat. Methods , vol.3 , pp. 303-313
    • Drew, D.1    Lerch, M.2    Kunji, E.3    Slotboom, D.J.4    de Gier, J.W.5
  • 8
    • 14144256100 scopus 로고    scopus 로고
    • An efficient strategy for high-throughput expression screening of recombinant integral membrane proteins
    • Eshaghi, S., Hedren, M., Nasser, M.I., Hammarberg, T., Thornell, A., and Nordlund, P. 2005. An efficient strategy for high-throughput expression screening of recombinant integral membrane proteins. Protein Sci. 14: 676-683.
    • (2005) Protein Sci , vol.14 , pp. 676-683
    • Eshaghi, S.1    Hedren, M.2    Nasser, M.I.3    Hammarberg, T.4    Thornell, A.5    Nordlund, P.6
  • 10
    • 9944233325 scopus 로고    scopus 로고
    • Crystallization informatics of membrane proteins
    • ed. S. Iwata, pp, International University Line, La Jolla, CA
    • Iwata, S. 2003. Crystallization informatics of membrane proteins. In Methods and results in crystallization of membrane proteins (ed. S. Iwata), pp. 283-297. International University Line, La Jolla, CA.
    • (2003) Methods and results in crystallization of membrane proteins , pp. 283-297
    • Iwata, S.1
  • 11
    • 33646011258 scopus 로고    scopus 로고
    • Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins
    • Kawate, T. and Gouaux, E. 2006. Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins. Structure 14: 673-681.
    • (2006) Structure , vol.14 , pp. 673-681
    • Kawate, T.1    Gouaux, E.2
  • 12
    • 0036427425 scopus 로고    scopus 로고
    • Importance of detergent and phospholipid in the crystallization of the human erythrocyte anion-exchanger membrane domain
    • Lemieux, M.J., Reithmeier, R.A., and Wang, D.N. 2002. Importance of detergent and phospholipid in the crystallization of the human erythrocyte anion-exchanger membrane domain. J. Struct. Biol. 137: 322-332.
    • (2002) J. Struct. Biol , vol.137 , pp. 322-332
    • Lemieux, M.J.1    Reithmeier, R.A.2    Wang, D.N.3
  • 13
    • 0345276579 scopus 로고    scopus 로고
    • Three-dimensional crystallization of the Escherichia coli glycerol-3-phosphate transporter: A member of the major facilitator superfamily
    • Lemieux, M.J., Song, J., Kim, M.J., Huang, Y., Villa, A., Auer, M., Li, X.D., and Wang, D.N. 2003. Three-dimensional crystallization of the Escherichia coli glycerol-3-phosphate transporter: A member of the major facilitator superfamily. Protein Sci. 12: 2748-2756.
    • (2003) Protein Sci , vol.12 , pp. 2748-2756
    • Lemieux, M.J.1    Song, J.2    Kim, M.J.3    Huang, Y.4    Villa, A.5    Auer, M.6    Li, X.D.7    Wang, D.N.8
  • 14
    • 0035853476 scopus 로고    scopus 로고
    • Monomeric state and ligand binding of recombinant GABA transporter from Escherichia coli
    • Li, X.D., Villa, A., Gownley, C., Kim, M.J., Song, J., Auer, M., and Wang, D.N. 2001. Monomeric state and ligand binding of recombinant GABA transporter from Escherichia coli. FEBS Lett. 494: 165-169.
    • (2001) FEBS Lett , vol.494 , pp. 165-169
    • Li, X.D.1    Villa, A.2    Gownley, C.3    Kim, M.J.4    Song, J.5    Auer, M.6    Wang, D.N.7
  • 15
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher, K.P., Lee, A.T., and Rees, D.C. 2002. The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism. Science 296: 1091-1098.
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 16
    • 0037391134 scopus 로고    scopus 로고
    • Membrane protein structural biology: The high-throughput challenge
    • Loll, P.J. 2003. Membrane protein structural biology: The high-throughput challenge. J. Struct. Biol. 142: 144-153.
    • (2003) J. Struct. Biol , vol.142 , pp. 144-153
    • Loll, P.J.1
  • 17
    • 33751290908 scopus 로고    scopus 로고
    • Structural genomics for membrane proteins
    • Lundstrom, K. 2006. Structural genomics for membrane proteins. Cell. Mol. Life Sci. 63: 2597-2607.
    • (2006) Cell. Mol. Life Sci , vol.63 , pp. 2597-2607
    • Lundstrom, K.1
  • 19
    • 0034986184 scopus 로고    scopus 로고
    • Determining the structure of biological macromolecules by transmission electron microscopy, single particle analysis and 3D reconstruction
    • Ruprecht, J. and Nield, J. 2001. Determining the structure of biological macromolecules by transmission electron microscopy, single particle analysis and 3D reconstruction. Prog. Biophys. Mol. Biol. 75: 121-164.
    • (2001) Prog. Biophys. Mol. Biol , vol.75 , pp. 121-164
    • Ruprecht, J.1    Nield, J.2
  • 20
    • 0035500087 scopus 로고    scopus 로고
    • A truncation of 2B subfamily cytochromes P450 yields increased expression levels, increased solubility, and decreased aggregation while retaining function
    • Scott, E.E., Spatzenegger, M., and Halpert, J.R. 2001. A truncation of 2B subfamily cytochromes P450 yields increased expression levels, increased solubility, and decreased aggregation while retaining function. Arch. Biochem. Biophys. 395: 57-68.
    • (2001) Arch. Biochem. Biophys , vol.395 , pp. 57-68
    • Scott, E.E.1    Spatzenegger, M.2    Halpert, J.R.3
  • 21
    • 23944491599 scopus 로고    scopus 로고
    • High-throughput solubility assay for purified recombinant protein immunogens
    • Stenvall, M., Steen, J., Uhlen, M., Hober, S., and Ottosson, J. 2005. High-throughput solubility assay for purified recombinant protein immunogens. Biochim. Biophys. Acta 1752: 6-10.
    • (2005) Biochim. Biophys. Acta , vol.1752 , pp. 6-10
    • Stenvall, M.1    Steen, J.2    Uhlen, M.3    Hober, S.4    Ottosson, J.5
  • 22
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. 2000. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405: 647-655.
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 23
    • 0035895353 scopus 로고    scopus 로고
    • Salt dependence of the formation and stability of the signaling state in G protein-coupled receptors: Evidence for the involvement of the Hofmeister effect
    • Vogel, R., Fan, G.B., Sheves, M., and Siebert, F. 2001. Salt dependence of the formation and stability of the signaling state in G protein-coupled receptors: Evidence for the involvement of the Hofmeister effect. Biochemistry 40: 483-493.
    • (2001) Biochemistry , vol.40 , pp. 483-493
    • Vogel, R.1    Fan, G.B.2    Sheves, M.3    Siebert, F.4
  • 25
    • 0037394496 scopus 로고    scopus 로고
    • Light scattering as a diagnostic for protein crystal growth-a practical approach
    • Wilson, W.W. 2003. Light scattering as a diagnostic for protein crystal growth-a practical approach. J. Struct. Biol. 142: 56-65.
    • (2003) J. Struct. Biol , vol.142 , pp. 56-65
    • Wilson, W.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.