메뉴 건너뛰기




Volumn 51, Issue 8, 2012, Pages 1625-1637

Imaging of protein crystals with two-photon microscopy

Author keywords

[No Author keywords available]

Indexed keywords

CHIRAL CRYSTALS; EXPERIMENTAL DATA; FLUORESCENT DYES; HIGH SIGNAL-TO-NOISE RATIO; INFRARED LIGHT; INVERSE CORRELATION; LYSOZYME CRYSTALS; NON DESTRUCTIVE; NONCENTROSYMMETRIC CRYSTALS; PROTEIN CRYSTAL; SECOND-ORDER NONLINEAR OPTICAL; SMALL PROTEIN CRYSTALS; THREE-PHOTON; TRYPTOPHAN RESIDUES; TWO PHOTON; TWO PHOTON MICROSCOPY; TWO-PHOTON EXCITED FLUORESCENCE; VISIBLE LIGHT;

EID: 84857575005     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201682q     Document Type: Article
Times cited : (27)

References (49)
  • 4
    • 75649119689 scopus 로고    scopus 로고
    • Nonlinear optical imaging of integral membrane protein crystals in lipidic mesophases
    • Kissick, D. J., Gualtieri, E. J., Simpson, G. J., and Cherezov, V. (2010) Nonlinear optical imaging of integral membrane protein crystals in lipidic mesophases Anal. Chem. 82, 491-497
    • (2010) Anal. Chem. , vol.82 , pp. 491-497
    • Kissick, D.J.1    Gualtieri, E.J.2    Simpson, G.J.3    Cherezov, V.4
  • 5
    • 77749237336 scopus 로고    scopus 로고
    • Evaluating the efficacy of tryptophan fluorescence and absorbance as a selection tool for identifying protein crystals
    • Gill, H. S. (2010) Evaluating the efficacy of tryptophan fluorescence and absorbance as a selection tool for identifying protein crystals Acta Crystallogr. F66, 364-372
    • (2010) Acta Crystallogr. , vol.66 , pp. 364-372
    • Gill, H.S.1
  • 6
    • 21644434938 scopus 로고    scopus 로고
    • An ultraviolet fluorescence-based method for identifying and distinguishing protein crystals
    • Judge, R. A., Swift, K., and Gonzalez, C. (2005) An ultraviolet fluorescence-based method for identifying and distinguishing protein crystals Acta Crystallogr. D61, 60-66
    • (2005) Acta Crystallogr. , vol.61 , pp. 60-66
    • Judge, R.A.1    Swift, K.2    Gonzalez, C.3
  • 7
    • 77950837302 scopus 로고    scopus 로고
    • Efficient UV detection of protein crystals enabled by fluorescence excitation at wavelengths longer than 300 nm
    • Dierks, K., Meyer, A., Oberthur, D., Rapp, G., Einspahr, H., and Betzel, C. (2010) Efficient UV detection of protein crystals enabled by fluorescence excitation at wavelengths longer than 300 nm Acta Crystallogr. F66, 478-484
    • (2010) Acta Crystallogr. , vol.66 , pp. 478-484
    • Dierks, K.1    Meyer, A.2    Oberthur, D.3    Rapp, G.4    Einspahr, H.5    Betzel, C.6
  • 9
    • 80053061272 scopus 로고    scopus 로고
    • Two-photon excited UV fluorescence for protein crystal detection
    • Madden, J. T., Dewalt, E. L., and Simpson, G. J. (2011) Two-photon excited UV fluorescence for protein crystal detection Acta Crystallogr. D67, 839-846
    • (2011) Acta Crystallogr. , vol.67 , pp. 839-846
    • Madden, J.T.1    Dewalt, E.L.2    Simpson, G.J.3
  • 11
    • 0842266594 scopus 로고    scopus 로고
    • Noninvasive two-photon imaging reveals retinyl ester storage structures in the eye
    • Imanishi, Y., Batten, M. L., Piston, D. W., Baehr, W., and Palczewski, K. (2004) Noninvasive two-photon imaging reveals retinyl ester storage structures in the eye J. Cell Biol. 164, 373-383
    • (2004) J. Cell Biol. , vol.164 , pp. 373-383
    • Imanishi, Y.1    Batten, M.L.2    Piston, D.W.3    Baehr, W.4    Palczewski, K.5
  • 12
    • 78650023050 scopus 로고    scopus 로고
    • Noninvasive multiphoton fluorescence microscopy resolves retinol and retinal condensation products in mouse eyes
    • Palczewska, G., Maeda, T., Imanishi, Y., Sun, W., Chen, Y., Williams, D. R., Piston, D. W., Maeda, A., and Palczewski, K. (2010) Noninvasive multiphoton fluorescence microscopy resolves retinol and retinal condensation products in mouse eyes Nat. Med. 16, 1444-1449
    • (2010) Nat. Med. , vol.16 , pp. 1444-1449
    • Palczewska, G.1    Maeda, T.2    Imanishi, Y.3    Sun, W.4    Chen, Y.5    Williams, D.R.6    Piston, D.W.7    Maeda, A.8    Palczewski, K.9
  • 13
    • 0037287759 scopus 로고    scopus 로고
    • Second harmonic generation imaging of endogenous structural proteins
    • Mohler, W., Millard, A. C., and Campagnola, P. J. (2003) Second harmonic generation imaging of endogenous structural proteins Methods 29, 97-109
    • (2003) Methods , vol.29 , pp. 97-109
    • Mohler, W.1    Millard, A.C.2    Campagnola, P.J.3
  • 14
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • Oesterhelt, D. and Stoeckenius, W. (1974) Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane Methods Enzymol. 31, 667-678
    • (1974) Methods Enzymol. , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 15
    • 70350074909 scopus 로고    scopus 로고
    • Lipidic sponge phase crystal structure of a photosynthetic reaction center reveals lipids on the protein surface
    • Wohri, A. B., Wahlgren, W. Y., Malmerberg, E., Johansson, L. C., Neutze, R., and Katona, G. (2009) Lipidic sponge phase crystal structure of a photosynthetic reaction center reveals lipids on the protein surface Biochemistry 48, 9831-9838
    • (2009) Biochemistry , vol.48 , pp. 9831-9838
    • Wohri, A.B.1    Wahlgren, W.Y.2    Malmerberg, E.3    Johansson, L.C.4    Neutze, R.5    Katona, G.6
  • 16
    • 0020475570 scopus 로고
    • Three-dimensional crystals of a membrane protein complex. The photosynthetic reaction centre from Rhodopseudomonas viridis
    • Michel, H. (1982) Three-dimensional crystals of a membrane protein complex. The photosynthetic reaction centre from Rhodopseudomonas viridis J. Mol. Biol. 158, 567-572
    • (1982) J. Mol. Biol. , vol.158 , pp. 567-572
    • Michel, H.1
  • 17
    • 57649118503 scopus 로고    scopus 로고
    • Heterologous expression and purification of the serotonin type 4 receptor from transgenic mouse retina
    • Salom, D., Wu, N., Sun, W., Dong, Z., Palczewski, K., Jordan, S., and Salon, J. A. (2008) Heterologous expression and purification of the serotonin type 4 receptor from transgenic mouse retina Biochemistry 47, 13296-13307
    • (2008) Biochemistry , vol.47 , pp. 13296-13307
    • Salom, D.1    Wu, N.2    Sun, W.3    Dong, Z.4    Palczewski, K.5    Jordan, S.6    Salon, J.A.7
  • 20
    • 67649392795 scopus 로고    scopus 로고
    • Crystallizing membrane proteins using lipidic mesophases
    • Caffrey, M. and Cherezov, V. (2009) Crystallizing membrane proteins using lipidic mesophases Nat. Protoc. 4, 706-731
    • (2009) Nat. Protoc. , vol.4 , pp. 706-731
    • Caffrey, M.1    Cherezov, V.2
  • 21
    • 0242385349 scopus 로고    scopus 로고
    • Detergents destabilize the cubic phase of monoolein: Implications for membrane protein crystallization
    • Misquitta, Y. and Caffrey, M. (2003) Detergents destabilize the cubic phase of monoolein: Implications for membrane protein crystallization Biophys. J. 85, 3084-3096
    • (2003) Biophys. J. , vol.85 , pp. 3084-3096
    • Misquitta, Y.1    Caffrey, M.2
  • 22
    • 0031751696 scopus 로고    scopus 로고
    • Obtaining crystal structures from bacterial photosynthetic reaction centers
    • Fritzsch, G. (1998) Obtaining crystal structures from bacterial photosynthetic reaction centers Methods Enzymol. 297, 57-77
    • (1998) Methods Enzymol. , vol.297 , pp. 57-77
    • Fritzsch, G.1
  • 25
    • 0013852463 scopus 로고
    • Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Å resolution
    • Blake, C. C., Koenig, D. F., Mair, G. A., North, A. C., Phillips, D. C., and Sarma, V. R. (1965) Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Å resolution Nature 206, 757-761
    • (1965) Nature , vol.206 , pp. 757-761
    • Blake, C.C.1    Koenig, D.F.2    Mair, G.A.3    North, A.C.4    Phillips, D.C.5    Sarma, V.R.6
  • 27
    • 77954438968 scopus 로고    scopus 로고
    • A dipicolinate lanthanide complex for solving protein structures using anomalous diffraction
    • Pompidor, G., Maury, O., Vicat, J., and Kahn, R. (2010) A dipicolinate lanthanide complex for solving protein structures using anomalous diffraction Acta Crystallogr. D66, 762-769
    • (2010) Acta Crystallogr. , vol.66 , pp. 762-769
    • Pompidor, G.1    Maury, O.2    Vicat, J.3    Kahn, R.4
  • 28
    • 0026566937 scopus 로고
    • Crystal structure disposition of thymidylic acid tetramer in complex with ribonuclease A
    • Birdsall, D. L. and McPherson, A. (1992) Crystal structure disposition of thymidylic acid tetramer in complex with ribonuclease A J. Biol. Chem. 267, 22230-22236
    • (1992) J. Biol. Chem. , vol.267 , pp. 22230-22236
    • Birdsall, D.L.1    McPherson, A.2
  • 30
    • 1942469425 scopus 로고    scopus 로고
    • Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center
    • Baxter, R. H., Ponomarenko, N., Srajer, V., Pahl, R., Moffat, K., and Norris, J. R. (2004) Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center Proc. Natl. Acad. Sci. U.S.A. 101, 5982-5987
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 5982-5987
    • Baxter, R.H.1    Ponomarenko, N.2    Srajer, V.3    Pahl, R.4    Moffat, K.5    Norris, J.R.6
  • 31
    • 33748878838 scopus 로고    scopus 로고
    • Spontaneous emission study of the femtosecond isomerization dynamics of rhodopsin
    • Kochendoefer, G. G. and Mathies, R. A. (1996) Spontaneous emission study of the femtosecond isomerization dynamics of rhodopsin J. Phys. Chem. 100, 14526-14532
    • (1996) J. Phys. Chem. , vol.100 , pp. 14526-14532
    • Kochendoefer, G.G.1    Mathies, R.A.2
  • 32
    • 0005401737 scopus 로고
    • Optical Second-Harmonic Generation in Crystalline Amino Acids
    • Rieckhoff, K. E. and Peticolas, W. L. (1965) Optical Second-Harmonic Generation in Crystalline Amino Acids Science 147, 610-611
    • (1965) Science , vol.147 , pp. 610-611
    • Rieckhoff, K.E.1    Peticolas, W.L.2
  • 33
    • 52049086426 scopus 로고    scopus 로고
    • Solution-state characteristics of the ultraviolet A-induced visible fluorescence from proteins
    • Guptasarma, P. (2008) Solution-state characteristics of the ultraviolet A-induced visible fluorescence from proteins Arch. Biochem. Biophys. 478, 127-129
    • (2008) Arch. Biochem. Biophys. , vol.478 , pp. 127-129
    • Guptasarma, P.1
  • 34
    • 0346100345 scopus 로고    scopus 로고
    • Free radical-mediated oxidation of free amino acids and amino acid residues in proteins
    • Stadtman, E. R. and Levine, R. L. (2003) Free radical-mediated oxidation of free amino acids and amino acid residues in proteins Amino Acids 25, 207-218
    • (2003) Amino Acids , vol.25 , pp. 207-218
    • Stadtman, E.R.1    Levine, R.L.2
  • 35
    • 78650747890 scopus 로고
    • The oxidation of tryptophan and some related compounds with persulphate
    • Boyland, E., Sims, P., and Williams, D. C. (1956) The oxidation of tryptophan and some related compounds with persulphate Biochem. J. 62, 546-550
    • (1956) Biochem. J. , vol.62 , pp. 546-550
    • Boyland, E.1    Sims, P.2    Williams, D.C.3
  • 37
    • 79955558728 scopus 로고    scopus 로고
    • Second harmonic generation imaging microscopy: Applications to diseases diagnostics
    • Campagnola, P. (2011) Second harmonic generation imaging microscopy: Applications to diseases diagnostics Anal. Chem. 83, 3224-3231
    • (2011) Anal. Chem. , vol.83 , pp. 3224-3231
    • Campagnola, P.1
  • 38
    • 84857622242 scopus 로고    scopus 로고
    • Structural changes in mixed Col I/Col v collagen gels probed by SHG microscopy: Implications for probing stromal alterations in human breast cancer
    • Ajeti, V., Nadiarnykh, O., Ponik, S. M., Keely, P. J., Eliceiri, K. W., and Campagnola, P. J. (2011) Structural changes in mixed Col I/Col V collagen gels probed by SHG microscopy: Implications for probing stromal alterations in human breast cancer Biomed. Opt. Express 2, 2307-2316
    • (2011) Biomed. Opt. Express , vol.2 , pp. 2307-2316
    • Ajeti, V.1    Nadiarnykh, O.2    Ponik, S.M.3    Keely, P.J.4    Eliceiri, K.W.5    Campagnola, P.J.6
  • 39
    • 79959518091 scopus 로고    scopus 로고
    • Second-order nonlinear optical imaging of chiral crystals
    • Kissick, D. J., Wanapun, D., and Simpson, G. J. (2011) Second-order nonlinear optical imaging of chiral crystals Annu. Rev. Anal. Chem. 4, 419-437
    • (2011) Annu. Rev. Anal. Chem. , vol.4 , pp. 419-437
    • Kissick, D.J.1    Wanapun, D.2    Simpson, G.J.3
  • 41
    • 0037879637 scopus 로고    scopus 로고
    • Point-group symmetry and physical properties of crystals
    • Klapper, H. and Hahn, T. (2006) Point-group symmetry and physical properties of crystals Int. Tables X-Ray Crystallogr. A, 804-808
    • (2006) Int. Tables X-Ray Crystallogr. A , pp. 804-808
    • Klapper, H.1    Hahn, T.2
  • 43
    • 3042828701 scopus 로고    scopus 로고
    • A novel UV laser-induced visible blue radiation from protein crystals and aggregates: Scattering artifacts or fluorescence transitions of peptide electrons delocalized through hydrogen bonding?
    • Shukla, A., Mukherjee, S., Sharma, S., Agrawal, V., Radha Kishan, K. V., and Guptasarma, P. (2004) A novel UV laser-induced visible blue radiation from protein crystals and aggregates: Scattering artifacts or fluorescence transitions of peptide electrons delocalized through hydrogen bonding? Arch. Biochem. Biophys. 428, 144-153
    • (2004) Arch. Biochem. Biophys. , vol.428 , pp. 144-153
    • Shukla, A.1    Mukherjee, S.2    Sharma, S.3    Agrawal, V.4    Radha Kishan, K.V.5    Guptasarma, P.6
  • 45
    • 79955788578 scopus 로고    scopus 로고
    • Solid-State NMR characterization of autofluorescent fibrils formed by the elastin-derived peptide GVGVAGVG
    • Sharpe, S., Simonetti, K., Yau, J., and Walsh, P. (2011) Solid-State NMR characterization of autofluorescent fibrils formed by the elastin-derived peptide GVGVAGVG Biomacromolecules 12, 1546-1555
    • (2011) Biomacromolecules , vol.12 , pp. 1546-1555
    • Sharpe, S.1    Simonetti, K.2    Yau, J.3    Walsh, P.4
  • 46
    • 58349088080 scopus 로고    scopus 로고
    • Fluorescence Investigations of Oxygen-Doped Simple Amine Compared with Fluorescent PAMAM Dendrimer
    • Chu, C. C. and Imae, T. (2009) Fluorescence Investigations of Oxygen-Doped Simple Amine Compared with Fluorescent PAMAM Dendrimer Macromol. Rapid Commun. 30, 89-93
    • (2009) Macromol. Rapid Commun. , vol.30 , pp. 89-93
    • Chu, C.C.1    Imae, T.2
  • 47
    • 80052538041 scopus 로고    scopus 로고
    • Computational Investigation of Amine-Oxygen Exciplex Formation
    • Haupert, L. M., Simpson, G. J., and Slipchenko, L. V. (2011) Computational Investigation of Amine-Oxygen Exciplex Formation J. Phys. Chem. A 115, 10159-10165
    • (2011) J. Phys. Chem. A , vol.115 , pp. 10159-10165
    • Haupert, L.M.1    Simpson, G.J.2    Slipchenko, L.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.