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Neutrons in Biology

A Perspective

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Book cover Neutrons in Biology

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

Abstract

After almost a decade of uncertainty, the field of neutrons in biology is set to embark on an era of stability and renewed vitality. As detailed in this volume, methodologies have been refined, new tools are now being added to the array, the two largest reactor sources have long term programs in place, and spallation sources are making an impact. By way of introduction, it is pertinent to reflect on the origins of the field and to highlight some aspects that have influenced the progress of the field. In an increasingly competitive environment, it is extremely important that the future capitalize on the substantial investment made over the last two to three decades.

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References

  • Alberi, J., (1976). Development of large-area, position-sensitive neutron detectors. In Neutron Scattering for the Analysis of Biological Structures. (B.P. Schoenborn, editor) VIII24–VIII42. (Nat. Technical Infor. Serv.; U.S. Dept. of Commerce, Springfield VA).

    Google Scholar 

  • Baldwin, J.P., Boseley, P.G., Bradbury, E.M., & Ibel, K., (1975). The subunit structure of the eukaryotic chromosome. Nature, 253:245–249.

    Article  PubMed  CAS  Google Scholar 

  • Bentley, G.A., & Mason, S.A., (1981). In Structural Studies on Molecules of Biological Interest (G. Dodson, J.P. Glusker and D. Sayre, editors) pp246–255. (Clarendon Press, Oxford).

    Google Scholar 

  • Bentley, G.A., Duee, E.D., Mason, S.A., & Nunes, A.C.J., (1979). Protein structure determination by neutron diffraction: lysozyme. Chim. Phys., 76:817–821.

    CAS  Google Scholar 

  • Bentley, G.A., Delepierre, M., Dobson, C.M., Wedin, R.E., Mason, S.A., & Poulsen, F.M.J., (1983). Exchange of individual hydrogens for a protein in a crystal and in solution. J. Mol. Biol., 170:243–247.

    Article  PubMed  CAS  Google Scholar 

  • Blasie, J.K., Pachence, J.M., & Herbette, L.G., (1984). Neutron diffraction and the decomposition of membrane scattering profiles into the scattering profiles of their molecular components. In Neutrons in Biology (B.P. Schoenborn, editor) pp201–210. (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Blasie, J.K., Schoenborn, B.P., & Zaccai, G., (1976). Direct methods for the analysis of lamellar neutron diffraction from oriented multilayers: A difference patterson deconvolution approach. In Neutron Scattering for the Analysis of Biological Structures (B.P. Schoenborn, editor) ppIII58–III67. (Nat. Technical Infor. Serv.; U.S. Dept. of Commerce, Springfield, VA).

    Google Scholar 

  • Bolton, W., Cox, J.M., & Perutz, M.F., (1968). Structure and function of haemoglobin IV. A three dimensional Fourier synthesis of horse deoxyhaemoglobin at 5.5Å resolution. J. Mol. Biol., 33:283–297.

    Article  PubMed  CAS  Google Scholar 

  • Bradshaw, J., (1995). Neutron diffraction studies of amphipathic helices in phospholipid bilayers. In Neutrons in Biology (B.P. Schoenborn and R. Knott, editors) (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Burks, C., & Engelman, D.M., (1981). Cholesteryl myristate conformation in liquid crystalline mesophases determined by neutron scattering. Proc. Natl. Acad. Sci. USA, 78:6863–6867.

    Article  PubMed  CAS  Google Scholar 

  • Cain, J.E., Norvell, J.C., & Schoenborn, B.P., (1976). Linear position-sensitive counter system for protein crystallography. In Neutron Scattering for the Analysis of Biological Structures. (B.P. Schoenborn, editor) ppVIII43–VIII50. (Nat. Technical Inform. Serv.; U.S. Dept. of Commerce, Springfield, VA).

    Google Scholar 

  • Capel, M., Moore, P.B., Engelman, D.M., Schneider, D., Schoenborn, B.P., Kjeldgaard, M., Langer, J., Ramakrishnan, V., Sillers, I.-Y., & Yabuki, S., (1987). Complete mapping of the proteins in the small ribosomal subunits of E.coli. Science, 238:1403–1406.

    CAS  Google Scholar 

  • Chabre, M., (1975). X-ray diffraction studies of retinal rods I. Structure of the disc membrane, effect of illumination. Biochim. Biophys. Acta, 382:322—355.

    Google Scholar 

  • Cheng, X., (1990). Hydration and solvent structure in proteins and solvent effect on protein refinement: a neutron diffraction study of myoglobin crystals. SUNY Stonybrook. Ph.D. Thesis.

    Google Scholar 

  • Cheng, X., & Schoenborn, B.P., (1990). Hydration in protein crystals. A neutron diffraction analysis of carbon-monoxymyoglobin. Acta Cryst., B46:195–208.

    CAS  Google Scholar 

  • Church, B., (1992). X-ray and Neutron Crystallography of Plastocyanin. University of Sydney NSW Australia. PhD Thesis.

    Google Scholar 

  • Convert, P., & Forsyth, J.B., (1983). Position-Sensitive Detection of Thermal Neutrons. (Academic Press, New York).

    Google Scholar 

  • Curmi, P.M.G., Stone, D.B., Schneider, D.K., & Mendelson, R.A., (1991). Mechanism of force generation studied by neutron scattering. Adv. Biophys., 27:131–141.

    Article  PubMed  CAS  Google Scholar 

  • Curmi, P.M.G., Stone, D.B., Schneider, D.K., Spudich, J.A., & Mendelson, R.A., (1988). Comparison of the structure of myosin subfragment 1 bound to actin and free in solution. A neutron scattering study using actin made ‘invisible’ by deuteration. J. Mol. Biol., 203:781–798.

    Article  PubMed  CAS  Google Scholar 

  • Cusack, S., (1984). Neutron scattering studies of virus structure. In Neutrons in Biology (B.P. Schoenborn, editor), pp 173–188. (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Engelman, D.M., & Moore, P.B., (1972). A new method for the determination of biological quarternary structure by neutron scattering. Proc. Natl. Acad. Sci. USA, 69:1997–1999.

    Article  PubMed  CAS  Google Scholar 

  • Engelman, D.M., Dianoux, A.J., Cusack, S., & Jacrot, B., (1984). Inelastic neutron scattering studies of hexoki-nase in solution. In Neutrons in Biology (B.P. Schoenborn, editor) pp365–380. (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Fischer, J., Radeka, V., & Boie, R.A., (1983). High position resolution and accuracy in 3He two-dimensional thermal neutron PSDs. In Position-Sensitive Detection of Thermal Neutrons (P. Convert and J.B. Forsyth, editors) pp 129–140. (Academic Press, London).

    Google Scholar 

  • Forsyth, V.T., Langan, P., Mahendrasingam, A., Fuller, W., & Mason, S.A., (1992). High-angle neutron fiber diffraction studies of DNA. Neutron News, 3(4):21–24.

    Article  Google Scholar 

  • Forsyth, V.T., Langan, P., Whalley, M.A., Mahendrasingam, A., Wilson, C.C., Giesen, U., Dauvergne, M.T., Mason, S.A., & Fuller, W., (1995). Time of flight Laue fiber diffraction studies of perdeuterated DNA. In Neutrons in Biology (B.P. Schoenborn and R. Knott, editors) (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Fuller, W., Forsyth, V. T., Mahendrasingam, A., Langan, P., & Pigram, W. J., (1995). DNA hydration studied by neutron fiber diffraction. In Neutrons in Biology (B.P. Schoenborn and R. Knott, editors) (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Garcia, A.E., Hummer, G., & Soumpasis, D.M., (1995). Theoretical description of biomolecular hydration — application to A-DNA. In Neutrons in Biology (B.P. Schoenborn and R. Knott, editors) (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Glinka, C.J., & Berk, N.F., (1983). The two-dimensional PSD at the National Bureau of Standards’ Small Angle Neutron Scattering Facility. In Position-Sensitive Detection of Thermal Neutrons. (P. Convert and J.B. Forsyth, editors), pp 141–148. (Academic Press, London).

    Google Scholar 

  • Graziano, V., Gerchman, S.E., Schneider, D.K., & Ramakrishnan, V.R., (1995). Neutron scattering studies on chromatin higher-order structure. In Neutrons in Biology (B.P. Schoenborn and R. Knott, editors) (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Gu, W., & Schoenborn, B.P., (1995). Molecular dynamics simulation of hydration in myoglobin. Proteins, 22:20–26.

    Article  PubMed  CAS  Google Scholar 

  • Hanson, J.C., & Schoenborn, B.P., (1981). Real space refinement of neutron diffraction data from sperm whale carbonmonoxymyoglobin. J. Mol. Biol., 153:117–146.

    Article  PubMed  CAS  Google Scholar 

  • Herbette, L., Napolitano, C.A., & McDaniel, R.V., (1984). Direct determination of the calcium profile structure for dipalmitoyllecithin multilayers using neutron diffraction. Biophys. J., 46:677–685.

    Article  PubMed  CAS  Google Scholar 

  • Herbette, L., DeFoor, P., Fleischer, S., Pascolini, D., Scarpa, A., & Blasie, J.K., (1985). The separate profile structures of the functional calcium pump protein and the phospholipid bilayer within isolated sarcoplasmic reticulum membranes determined by X-ray and neutron diffraction. Biochim. Biophys. Acta, 817:103–122.

    Article  PubMed  CAS  Google Scholar 

  • Hjelm, R.P., Kneale, G.G., Suau, P., Baldwin, J.P., Bradbury, E.M., & Ibel, K., (1977). Small angle neutron scattering studies of chromatin subunits in solution. Cell, 10:139–151.

    Article  PubMed  CAS  Google Scholar 

  • Ibel, K., & Stuhrmann, H.B., (1975). Comparison of neutron and X-ray scattering of dilute myoglobin solutions. J. Mol. Biol., 93:255–265.

    Article  PubMed  CAS  Google Scholar 

  • Jacrot, B., & Zaccai, G., (1981). Determination of molecular weight by neutron scattering. Biopolymers, 20:2413–2426.

    Article  CAS  Google Scholar 

  • Jiang, J., & Brünger, A.T., (1994). Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures. J. Mol. Biol., 243:100–115.

    Article  PubMed  CAS  Google Scholar 

  • King, G.I., & Schoenborn, B.P., (1985). Neutron scattering of bacteriorhodopsin. Methods Enzymol., 88:241–248.

    Article  Google Scholar 

  • King, G.I., Stoeckenius, W., Crespi, H.L., & Schoenborn, B.P., (1979). The location of low retinal in the purple membrane profile by neutron diffraction. J. Mol. Biol., 130:395–404.

    Article  PubMed  CAS  Google Scholar 

  • King, G.I., Chao, N.-M., & White, S.H., (1984). Neutron diffraction studies on incorporation of hexane into oriented lipid bilayers. In Neutrons in Biology (B.P. Schoenborn, editor) ppl59–172. (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Knott, R. (1995). Neutron scattering in Australia. In Neutrons in Biology (B.P. Schoenborn and R. Knott, editors) (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Kossiakoff, A.A., (1983). Protein dynamics investigated by the neutron diffraction-hydrogen exchange technique. Nature, 296:713–721.

    Article  Google Scholar 

  • Kossiakoff, A.A., & Shteyn, S., (1984). Effect of protein packing structure on side-chain methyl rotor conformations. Nature, 311:582–583.

    Article  PubMed  CAS  Google Scholar 

  • Kossiakoff, A.A., & Spencer, S.A., (1980). Neutron diffraction identifies His57 as the catalytic base in trypsin. Nature, 288:414–416.

    Article  PubMed  CAS  Google Scholar 

  • Kossiakoff, A.A., & Spencer, S.A., (1981). Direct determination of the protonation states of aspartic acid-102 and histidine-57 in the tetrahedral intermediate of the serine proteases. Biochem., 20:6462–6474.

    Article  CAS  Google Scholar 

  • Langan, P., Forsyth, V.T., Mahendrasingam, A., Alexeev, D., Mason, S.A., & Fuller, W., (1993). In Water-Bio-molecule Interactions. Conference Proceedings (M.U. Palma, M.B. Palma-Vittorelli and F. Parak, editors) pp235–238. (SIF, Bologna).

    Google Scholar 

  • Lehman, M.S., & Zaccai, G., (1984). Neutron small-angle scattering studies of ribonuclease in mixed aqueous solutions and determination of the preferentially bound water. Biochem., 23:1939–1942.

    Article  Google Scholar 

  • Lynn, J.W., Kjems, J.K., Passell, L., Saxena, A.M., & Schoenborn, B.P., (1976). Iron-germanium multilayer neutron polarizing monochromators. J. Appl. Cryst., 9:454–459.

    Article  Google Scholar 

  • Marguerie, G., & Stuhrmann, H.B., (1976). A neutron small-angle scattering study of bovine fibrinogen. J. Mol. Biol., 102:143–156.

    Article  PubMed  CAS  Google Scholar 

  • Mason, S.A., Bentley, G.A., & McIntyre, G.J., (1984). Deuterium exchange in lysozyme at 1.4Å resolution. In Neutrons in Biology (B.P. Schoenborn, editor) pp323–334. (Plenum Publishing Corporation, New York).

    Google Scholar 

  • May, R.P., Stuhrmann, H.B., & Nierhaus, K.H., (1984). Structural elements of the 50S subunit of E.coli ribosomes. In Neutrons in Biology (B.P. Schoenborn, editor) pp25–46. (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Mezei, F., (1994). On the comparison of continuous and pulsed sources. Neutron News, 5:2–3.

    Article  Google Scholar 

  • Middendorf, H.D., (1984). Inelastic scattering from biomolecules: Principles and prospects. In Neutrons in Biology (B.P. Schoenborn, editor) pp401–437. (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Middendorf, H.D., Randell, J.T., & Crespi, H., (1984). Neutron spectroscopy of hydrogeneous and biosynthetically deuterated proteins. In Neutrons in Biology (B.P. Schoenborn, editor) pp381–400. (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Moore, F.M., Willis, B.T.M., & Crawfoot-Hodgkin, D., (1967). Crystal and molecular structure from neutron diffraction analysis. Nature, 214:130–133.

    Article  PubMed  CAS  Google Scholar 

  • Nambudripad, R., Stark, W., Opella, S.J., & Makowski, L., (1991). Membrane-mediated assembly of filamentous bacteriophage Pf1 coat protein. Science, 252:1305–1308.

    Article  PubMed  CAS  Google Scholar 

  • Niimura, N., (1995a). Neutron scattering and diffraction instrumentation for structural biology in Japan. In Neutrons in Biology. (B.P. Schoenborn and R. Knott, editors) (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Niimura, N., (1995b). Neutron diffractometer for bio-crystallography (BIX) with an imaging plate neutron detector. In Neutrons in Biology. (B.P. Schoenborn and R. Knott, editors) (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Nobbs, C.L., Watson, H.C., & Kendrew, J.C., (1966). Structure of deoxymyoglobin: A crystallographic study. Nature, 209:339–341.

    Article  PubMed  CAS  Google Scholar 

  • Pardon, J.F., Worcester, D.L., Wooley, J.C., Tatchell, K., van Holde, K.E., & Richards, B.M., (1975). Low angle neutron scattering from chromatin subunit particles. Nucleic Acids Res., 2:2163–2176.

    Article  PubMed  CAS  Google Scholar 

  • Phillips, S.E.V., & Schoenborn, B.P., (1981). Neutron diffraction reveals oxygen-histidine hydrogen bond in oxymyoglobin. Nature, 292:81–82.

    Article  PubMed  CAS  Google Scholar 

  • Pynn, R., (1995). LANSCE expands future operations. Neutron News, 6(1):30.

    Google Scholar 

  • Radeka, V., Schaknowski, N.A., Smith, G.C., & Yu, B., (1995). High precision thermal neutron detectors. In Neutrons in Biology (B.P. Schoenborn and R. Knott, editors) (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Raghavan, N.V., & Schoenborn, B.P., (1984). The structure of bound water and refinement of acid metmyoglobin. In Neutrons in Biology (B.P. Schoenborn, editor) pp247–259. (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Ramakrishnan, V.R., Finch, J.T., Graziano, V., Lee, P.L., & Sweet, R.M., (1993). Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. Nature, 362:219–223.

    Article  PubMed  CAS  Google Scholar 

  • Savage, H.F.J., & Wlodawer, A., (1986). Determination of water structure around biomolecules using X-ray and neutron diffraction methods. Methods Enzymol., 127:162–183.

    Article  PubMed  CAS  Google Scholar 

  • Saxena, A.M., & Majkrzak, C.F., (1984). Neutron optics with multilayer monochromators. In Neutrons in Biology. (B.P. Schoenborn, editor) ppl43–158. (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Saxena, A.M., & Schoenborn, B.P., (1976). Multilayer monochromators for neutron scattering. In Neutron Scattering for the Analysis of Biological Structures (B.P. Schoenborn, editor) ppVII30–VIII48. (Nat. Technical Infor. Serv.; U.S. Dept. of Commerce, Springfield, VA).

    Google Scholar 

  • Saxena, A.M., & Schoenborn, B.P., (1977). Multilayer neutron monochromators. Acta Cryst., 833:805–813.

    Google Scholar 

  • Saxena, A.M., & Schoenborn, B.P, (1988). Multilayer monochromators for neutron spectrometers. Material Science Forum, 27/28:313–318.

    Article  Google Scholar 

  • Schoenborn, B.P., (1965). Binding of xenon to haemoglobin. Nature, 208:760–762.

    Article  PubMed  CAS  Google Scholar 

  • Schoenborn, B.P., (1969a). Neutron diffraction analysis of myoglobin. Nature, 224:143–146.

    Article  PubMed  CAS  Google Scholar 

  • Schoenborn, B.P., (1969b). Structure of alkaline metmyoglobin-xenon complex. J. Mol. Biol., 45:279–303.

    Article  Google Scholar 

  • Schoenborn, B.P., (1972). A neutron diffraction analysis of myoglobin II. Hydrogen-deuterium bonding in the main chain. In Structure and Function of Oxidation Reduction Enzymes (A. Akeson and A. Ehrenberg, editors) ppl09–116. (Pergamon Press, Oxford).

    Google Scholar 

  • Schoenborn, B.P., (1975). In Anomalous Scattering (S. Ramaseshan and S.C. Abrahams, editors) pp407–421. (Munksgaard, Copenhagen).

    Google Scholar 

  • Schoenborn, B.P., (1976a). Neutron scattering for the analysis of membranes. Biochim. Biophys. Acta, 457:41–55.

    Article  PubMed  CAS  Google Scholar 

  • Schoenborn, B.P., (1976b). Neutron Scattering for the Analysis of Biological Structures. (Nat. Technical Infor. Serv.; U.S. Dept. of Commerce, Springfield, VA).

    Google Scholar 

  • Schoenborn, B.P., (1983a). Peak shape analysis for protein neutron crystallography with position-sensitive detectors. Acta Cryst., A39:315–321.

    CAS  Google Scholar 

  • Schoenborn, B.P., (1983b). Data processing in neutron protein crystallography using position-sensitive detectors. In Position-Sensitive Detection of Thermal Neutrons (P. Convert and J.B. Forsyth, editors) pp321–331. (Academic Press, London).

    Google Scholar 

  • Schoenborn, B.P., (1984). Neutrons in Biology. (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Schoenborn, B.P., (1988). The solvent effect in protein crystals. A neutron diffraction analysis of solvent and ion density. J. Mol. Biol., 201:741–749.

    Article  PubMed  CAS  Google Scholar 

  • Schoenborn, B.P., (1992a). Area detectors for neutron protein crystallography. SPIE, 1737:235–243.

    Article  Google Scholar 

  • Schoenborn, B.P., (1992b). Multilayer monochromators and super mirrors for neutron protein crystallography using a quasi Laue technique. SPIE, 1738:192–199.

    Article  CAS  Google Scholar 

  • Schoenborn, B.P., & Nunes, A.C., (1972). Neutron scattering. Ann. Rev. Biophys. Bioengineer., 1:529–552.

    Article  CAS  Google Scholar 

  • Schoenborn, B.P., & Pitcher, E., (1995). Neutron diffractometers for structural biology at spallation neutron sources. In Neutrons in Biology (B.P. Schoenborn and R. Knott, editors) (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Schoenborn, B.P., Caspar, D.L.D., & Kammerer, P.F.J., (1974). A novel neutron monochromator. J. Appl. Cryst., 7:508–510.

    Article  Google Scholar 

  • Schoenborn, B.P., Nunes, A.C., & Nathans, R., (1970). Neutron diffraction analysis of biological structures. Berichte Bunsengessellschaft fur Physical Chemistry, 74:1202–1207.

    CAS  Google Scholar 

  • Schoenborn, B.P., Watson, H.C., & Kendrew, J.C., (1965). Binding of xenon to sperm whale myoglobin. Nature, 207:28–30.

    Article  PubMed  CAS  Google Scholar 

  • Schoenborn, B.P., Alberi, J., Saxena, A.M., & Fischer, J.J., (1978). Alow angle neutron data acquisition system for molecular biology. J. Appl. Cryst., 11:455–460.

    Article  CAS  Google Scholar 

  • Seeger, P.A., & Hjelm, R.P., (1991). Small-angle neutron scattering at pulsed spallation sources. J. Appl. Cryst., 24:467–478.

    Article  Google Scholar 

  • Shu, F., (1994). The Structure of Solvent Molecules Bound to Per-Deuterated, Recombinant Sperm-Whale Myoglobin. SUNY Stonybrook. Ph.D. Thesis.

    Google Scholar 

  • Stark, W., Glucksman, M.J., & Makowski, L., (1988). Conformation of the coat protein of filamentous bacteriophage Pfl determined by neutron diffraction from magnetically oriented gels of specifically deuterated virons. J. Mol. Biol., 199:171–182.

    Article  PubMed  CAS  Google Scholar 

  • Stuhrmann, H.B., (1973). Comparison of the three basic scattering functions of myoglobin in solution with those from the known structure in crystalline state. J. Mol. Biol., 77:363–369.

    Article  PubMed  CAS  Google Scholar 

  • Stuhrmann, H.B., (1974). Neutron small-angle scattering of biological macromolecules in solution. J. Appl. Cryst., 7:173–178.

    Article  CAS  Google Scholar 

  • Teeter, M.M., (1984). Water structure of a hydrophobic protein at atomic resolution: Pentagon rings of water molecules in crystals of crambin. Proc. Natl. Acad. Sci. USA, 81:6014–6018.

    Article  PubMed  CAS  Google Scholar 

  • Teeter, M.M., & Kossiakoff, A.A., (1984). The neutron structure of the hydrophobic plant protein crambin. In Neutrons in Biology (B.P. Schoenborn, editor) pp335–348. (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Timmins, P.A., (1988). Neutron scattering studies of the structure and assembly of spherical viruses. Makromol. Chem. Makromol. Symp., 15:311–321.

    Article  Google Scholar 

  • Timmins, P.A., (1995). Low resolution neutron crystallography of large biological macromolecular assemblies. Neutron News, 6(1):13–18.

    Article  Google Scholar 

  • Timmins, P.A., & Pebay-Peyroula, E., (1995). Protein-detergent interactions in single crystals of membrane proteins studied by neutron crystallography. In Neutrons in Biology (B.P. Schoenborn and R. Knott, editors) (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Timmins, P.A., Wild, J., & Witz, J., (1994). The three-dimensional distribution of RNA and protein in the interior of tomato bushy stunt virus: A neutron low-resolution single-crystal diffraction study. Structure, 2:1191–1201.

    Article  PubMed  CAS  Google Scholar 

  • Timmins, P.A., Poliks, B., & Banaszak, L.J., (1992). The location of bound lipid in the lipovitellin complex. Science, 257:652–655.

    Article  PubMed  CAS  Google Scholar 

  • Trewhella, J., Gogel, E., Zaccai, G., & Engelman, D.M., (1984). Neutron diffraction studies of bacteriorhodopsin structure. In Neutrons in Biology (B.P. Schoenborn, editor) pp227–246 (Plenum Publishing Corporation, New York).

    Google Scholar 

  • White, S.H., & Wiener, M.C., (1995). Fluid bilayer structure determination: joint refinement in ‘composition space’ using X-ray and neutron diffraction data. In Neutrons in Biology (B.P. Schoenborn and R. Knott, editors) (Plenum Publishing Corporation, New York).

    Google Scholar 

  • White, S.H., King, G.I., & Cain, J.E., (1981). Location of hexane in lipid bilayers determined by neutron diffraction. Nature, 290:161–163.

    Article  CAS  Google Scholar 

  • Wiener, M.C., & White, S.H., (1991a). Fluid bilayer structure determination by the combined use of X-ray and neutron diffraction. I. Fluid bilayer models and the limit of resolution. Biophys. J., 59:162–173.

    Article  PubMed  CAS  Google Scholar 

  • Wiener, M.C., & White, S.H., (1991b). Fluid bilayer structure determination by the combined use of X-ray and neutron diffraction. II. ‘Composition-space’ refinement method. Biophys. J., 59:174–185.

    Article  PubMed  CAS  Google Scholar 

  • Wilson, C.C., (1995). The potential for biological structure determination with pulsed neutrons. In Neutrons in Biology (B.P. Schoenborn and R. Knott, editors) (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Wise, D.S., Karlin, A., & Schoenborn, B.P., (1979). An analysis by low-angle neutron scattering of the structure of the acetylcholine receptor from torpedo californica in detergent solution. Biophys. J., 28:473–496.

    Article  PubMed  CAS  Google Scholar 

  • Wlodawer, A., & Sjölin, L., (1984). Application of joint neutron and X-ray refinement to the investigation of the structure of ribonuclease A at 2.0Å resolution. In Neutrons in Biology (B.P. Schoenborn, editor) pp349–364. (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Wlodawer, A., Miller, M., & Sjölin, L., (1983). Active site of RNase: Neutron diffraction study of a complex with uridine vanadate, a transition-state analog. Proc. Natl. Acad. Sci. USA, 80:3628–3631.

    Article  PubMed  CAS  Google Scholar 

  • Wlodawer, A., Walter, J., Huber, R., & Sjölin, L., (1984). Structure of bovine pancreatic trypsin inhibitor. Results of joint neutron and X-ray refinement of crystal form II. J. Mol. Biol., 180:301–329.

    Article  PubMed  CAS  Google Scholar 

  • Worcester, D.L., (1975). In Biological Membranes (D. Chapman and D.F.H. Wallach, editors) pp1–48. (Academic Press, London).

    Google Scholar 

  • Worcester, D.L., (1976). Neutron diffraction studies of biological membranes and membrane components. In Neutron Scattering for the Analysis of Biological Structures (B.P. Schoenborn, editor) ppIII37–III57. (Nat. Technical Infor. Serv.; U.S. Dept. of Commerce, Springfield, VA).

    Google Scholar 

  • Worcester, D.L., & Franks, N.P., (1976). Structural analysis of hydrated egg lecithin and cholesterol bilayers. II. Neutron diffraction. J. Mol. Biol., 100:359–378.

    Article  PubMed  CAS  Google Scholar 

  • Worcester, D.L., Harnacher, K., Kaiser, H., Kulasekere, R., & Torbet, J., (1995). Intercalation of small hydrophobic molecules in lipid bilayers containing cholesterol. In Neutrons in Biology (B.P. Schoenborn and R. Knott, editors) (Plenum Publishing Corporation, New York).

    Google Scholar 

  • Yeager, M., (1976). Neutron diffraction analysis of the structure of retinal photoreceptor membranes and rhodopsin. In Neutron Scattering for the Analysis of Biological Structures. (B.P. Schoenborn, editor) ppIII3–III36. (Nat. Technical Infor. Serv.; U.S. Dept. of Commerce, Springfield, VA).

    Google Scholar 

  • Yeager, M., Schoenborn, B.P., Engelman, D.M., Moore, P.B., & Stryer, L., (1980a). Neutron diffraction of intact retinas. J. Mol. Biol., 137:1–34.

    Article  Google Scholar 

  • Yeager, M., Schoenborn, B.P., Engelman, D.M., Moore, P.B., & Stryer, L., (1980b). Neutron diffraction analysis of the structure of rod photoreceptor membranes in intact retinas. J. Mol. Biol., 137:315–348.

    Article  PubMed  CAS  Google Scholar 

  • Zaccai, G., Blasie, J.K., & Schoenborn, B.P., (1975). Neutron diffraction studies on the location of water in lecithin bilayers. Proc. Natl. Acad. Sci. USA, 72:376–380.

    Article  PubMed  CAS  Google Scholar 

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Authors and Affiliations

  1. Australian Nuclear Science and Technology Organization, Private Mail Bag, Menai, NSW, 2234, Australia

    R. B. Knott

  2. B. P. Schoenborn, Los Alamos National Laboratory, Los Alamos, New Mexico, 87545, USA

    B. P. Schoenborn

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  1. R. B. Knott
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  2. B. P. Schoenborn
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Editors and Affiliations

  1. Los Alamos National Laboratory, Los Alamos, New Mexico, USA

    Benno P. Schoenborn

  2. Australian Nuclear Science and Technology Organisation, Menai, New South Wales, Australia

    Robert B. Knott

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Knott, R.B., Schoenborn, B.P. (1996). Neutrons in Biology. 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_1

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  • DOI: https://doi.org/10.1007/978-1-4615-5847-7_1

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