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In Situ Shape and Distance Measurements in Neutron Scattering and Diffraction

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Neutrons in Biology

Part of the book series: Basic Life Sciences ((BLSC,volume 64))

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Abstract

Neutron scattering combined with selective isotopic labeling and contrast matching is useful for obtaining in situ structural information about a selected particle, or particles, in a macromolecular complex. The observed intensities, however, may be distorted by inter-complex interference and by scattering-length-density fluctuations of the (otherwise) contrast-matched portions. Methods have been proposed to cancel out such distortions (Hoppeā€™s method, the Statistical Labeling Method, and the Triple Isotopic Substitution Method). With these methods as well as related unmixed-sample methods, structural information about the selected particle(s) can be obtained without these distortions. We have generalized these methods so that, in addition to globular particles in solution, they can be applied to in situ structures of systems having underlying symmetry and/or net orientation as well. The information obtainable from such experiments is discussed.

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References

  • Capel, M.S., Engelman, D.M., Freeborn, B.R., Kjeldgaard, M., Langer, J.A., Ramakrishnan, V., Schindler, D.G., Schneider, D.K., Schoenborn, B.P., Sillers, I.-Y., Yabuki, S., & Moore, P.B., (1987). A complete mapping of the proteins in the small ribosomal subunit of Escherichia coli. Science, 238:1403ā€“1406.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  • Curmi, P.M.G., & Mendelson, R.A., (1991). Neutron diffraction intensities from arrays of isotopically substituted particles in an invisible matrix. J. Appl. Cryst., 24:312ā€“315.

    ArticleĀ  CASĀ  Google ScholarĀ 

  • Engelman, D.M., & Moore, P.B., (1972). Anew method for the determination of biological quaternary structure by neutron scattering. Proc. Natl. Acad. Sci. USA, 69:1997ā€“1999.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  • Fujiwara, S., & Mendelson, R.A., (1994). The statistical labeling method and in situ neutron scattering and diffraction measurements on ordered systems. J. Appl. Cryst., 27:912ā€“923.

    ArticleĀ  CASĀ  Google ScholarĀ 

  • Fujiwara, S., Stone, D.B., & Mendelson, R.A., (1994). Measurement of inter-RLC distance in scallop myosin by neutron scattering. Biophys. J., 66:a76.

    Google ScholarĀ 

  • Harrison, D.H., May, R.P., & Moore, P.B., (1993). Measurement of the radii of gyration of ribosomal components in situ by neutron scattering. J. Appl. Cryst., 26:198ā€“206.

    ArticleĀ  CASĀ  Google ScholarĀ 

  • Hoppe, W., (1972). A new X-ray method for the determination of the quaternary structure of protein complexes. Israel J. Chem., 10:321ā€“333.

    CASĀ  Google ScholarĀ 

  • Hoppe, W., (1973). The label triangulation method and the mixed isomorphous replacement principle. J. Mol. Biol., 78:581ā€“585.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  • Hoppe, W., May, R., Stƶckel, P., Lorenz, S., Erdmann, V.A., Wittmann, H.G., Crespi, H.L., Katz, J.J., & Ibel, K., (1975). Neutron scattering measurements with the label triangulation method on the 50 S subunit of E. coli ribosomes. Brookhaven Symp. Biol., 27:IV 38ā€“48.

    Google ScholarĀ 

  • Kneale, G.G., Baldwin, J.P., & Bradbury, E.M., (1977). Neutron scattering studies of biological macromolecules in solution. Q. Rev. Biophys., 10:485ā€“527.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  • Moore, P.B., & Engelman, D.M., (1977). Model calculations of protein pair interference functions. J. Mol. Biol., 112:228ā€“234.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  • Pavlov, M.Yu., & Serdyuk, I.N., (1987). Three-isotopic-substitutions method in small-angle neutron scattering. J. Appl. Cryst., 20:105ā€“110.

    ArticleĀ  CASĀ  Google ScholarĀ 

  • Pavlov, M.Yu., Rublevskaya, I.N., Serdyuk, I.N., ZaccaĆÆ, G., Leberman, R., & Ostanevich, Yu.M., (1991). Experimental verification of the triple isotopic substitution method in small-angle neutron scattering. J. Appl. Cryst., 24:243ā€“254.

    ArticleĀ  Google ScholarĀ 

  • Ramakrishnan, V.R., & Moore, P.B., (1981). Analysis of neutron distance data. J. Mol. Biol., 153:719ā€“738.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  • Serdyuk, I.N., & Pavlov, M.Yu., (1988). Anew approach in small-angle neutron scattering: a method of triple isotopic substitutions. Makromol. Chem., 15:167ā€“184.

    ArticleĀ  Google ScholarĀ 

  • Serdyuk, I.N., Pavlov, M.Yu., Rublevskaya, I.N., ZaccaĆÆ, G., & Leberman, R., (1994). The triple isotopic substitution method in small angle neutron scattering. Application to the study of the ternary complex EF-TuĀ·GT-PĀ·aminoacyl-tRNA. Biophys. Chem., 53:123ā€“130.

    ArticleĀ  PubMedĀ  CASĀ  Google ScholarĀ 

  • Stƶckel, P., May, R., Strell, I., Cejka, Z., Hoppe, W., Heumann, H., Zillig, W., & Crespi, H.L., (1980a). The core subunit structure in RNA polymerase holoenzyme determined by neutron small-angle scattering. Eur. J. Biochem., 112:411ā€“417.

    ArticleĀ  PubMedĀ  Google ScholarĀ 

  • Stƶckel, P., May, R., Strell, I., Cejka, Z., Hoppe, W., Heumann, H., Zillig, W., & Crespi, H.L., (1980b). The subunit positions within RNA polymerase holoenzyme determined by triangulation of centre-to-centre distances. Eur. J. Biochem., 112:419ā€“423.

    ArticleĀ  PubMedĀ  Google ScholarĀ 

  • Stƶckel, P., May, R., Strell, I., Cejka, Z., Hoppe, W., Heumann, H., Zillig, W., Crespi, H.L., Katz, J.J., & Ibel, K., (1979). Determination of intersubunit distances and subunit shape parameters in DNA-dependent RNA polymerase by neutron small-angle scattering. J. Appl. Cryst., 12:176ā€“185.

    ArticleĀ  Google ScholarĀ 

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Fujiwara, S., Mendelson, R.A. (1996). In Situ Shape and Distance Measurements in Neutron Scattering and Diffraction. In: Schoenborn, B.P., Knott, R.B. (eds) Neutrons in Biology. Basic Life Sciences, vol 64. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5847-7_33

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  • DOI: https://doi.org/10.1007/978-1-4615-5847-7_33

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-7680-4

  • Online ISBN: 978-1-4615-5847-7

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