Synchrotron radiation in the biosciences

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書誌事項

Synchrotron radiation in the biosciences

edited by B. Chance ... [et al.]

Clarendon Press, c1994

大学図書館所蔵 件 / 全18件

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注記

Includes bibliographical references and index

内容説明・目次

内容説明

During the past decade a substantial number of synchrotron facilities have been established worldwide. The extraordinary and unique characteristics of synchrotron radiation in terms of brightness, collimation, and unlimited tunability have opened up tremendous opportunities for biosciences, notably in the study of the structures, functions, and dynamics of biological objects. This book presents state-of-the-art reviews and up-to-date progress reports on the use of sychrotron radiation for research in the biosciences. It is based on lectures presented at the Fourth International Conference on Biophysics and Synchrotron Radiation which was held in Tsukuba, Japan, under the auspices of the Japanese Biophysical Society, in 1992. It discusses advances in the application of synchrotron radiation to biophysics and medicine, of interest to researchers from many diverse fields. Since the first application of synchrotron radiation to biology in the 1970s for X-ray diffraction from muscle, the field has advanced considerably. One recent application is X-ray micro-imaging. This permits imaging of unstained, wet, and unsectioned biospecimens, allowing observation of living cells. Medical advances include angiography and computerized tomography. The volume is divided into nine parts covering the following topics: crystallographic studies on macromolecular structure, solution X-ray scattering, biology with neutron radiation, biological X-ray absorption fine structure spectroscopy, X-ray beamlines and detectors, structural studies on muscle proteins, muscle contraction, and filamentous viruses, X-ray microimaging, medical applications of synchrotron radiation: angiography, computerized tomography, and others, and radiation biophysics using synchrotron radiation.

目次

List of contributors. Part I: Crystallographic studies on macromolecular structure. 1.1: Recent developments in studies of macromolecular structure by X-ray crystallography. 1.2: Time-resolved macromolecular crystallography. 1.3: Protein crystallography in Japan. 1.4: Experience in the measurement and analysis of multiwavelength anomalous dispersion data from macromolecular crystals. 1.5: Electrostatic interactions and conformational variability in cubic insulin crystals. 1.6: Crystal structural analysis of tobacco necrosis virus (TNV). 1.7: Cryocrystallography of native and derivatized ribosomal crystals. 1.8: Structure and function of glutathione synthetase from Escherichia coli B. 1.9: Protein structure analyses exploiting the data collection efficiency and precision provided by the macromolecule-oriented Weissenberg camera installed at Beamline 6A2 of the Photon Factory, Tsukuba. 1.10: Structure and function of carbonic anhydrase: synchrotron X-ray diffraction studies of human carbonic anhydrase I and inhibitor complexes. 1.11: Structure study of hydrogenase and related proteions in sulfate-reducing bacteria. 1.12: 'Pivot hypothesis': a signalling mechanism in a bacterial chemotaxis receptor. 1.13: Fast Weissenberg data collection as an altrnative to the Laue method in kinetic crystallography. Part 2: More information and time-dependent studies from solution X-ray scattering. 2.1: Solution scattering. 2.2: Time-resolved X-ray scattering study of the allosteric transition of Escherichia coli aspartate transcarbamylase. 2.3: The effect of point mutations on the conformational changes of the allosteric enzyme aspartate transcarbamylase from Escherichia coli. 2.4: Dynamics of microtubules from stochastic switching to periodic swinging. 2.5: Synchrotron radiation X-ray diffraction and cryo electron microscopy studies of vinblastine-induced polymers of purified tubulin: evaluation of the effects of magnesium concentration and temperature. 2.6: Expression of function of calmodulin: interaction between calmodulin fragment and mastoparan. 2.7: Use of X-ray solution scattering for a protein folding study. 2.8: High-resolution small-angle synchrotron X-ray diffraction study on multilamellar phospholipid systems. 2.9: Temperature-jump relaxation studies on phospholipids: structural intermediates and memory effect in phase transitions. Part 3: Biology with neutron radiation. 3.1: Neutrons in biology - complementarity with X-rays. 3.2: Hydrogen bonding and solvent in proteins. 3.3: Neutron and X-ray scattering studies of the interactions between Ca2+-binding proteins and their regulatory targets: comparisons of troponin C and calmodulin. 3.4: Characteristic structure of phosphatidylinositol diphosphate (PIP2) complex with bovine serum albumin and water in PIP2 bilayers. Part 4: Recent developments in biological X-ray absorption fine-structure spectroscopy. 4.1: Sensitive and rapid biological X-ray absorption fine-structure spectroscopy. 4.2: X-ray absorption spectroscopy using high-brilliance photon sources. 4.3: X-ray studies of some metalloproteins. 4.4: A structural model for the photosynthetic oxygen-evolving manganese complex. 4.5: X-ray absorption fine structure spectroscopy and electron paramagnetic resonance studies on the molecular structure and electronic state of the Mn cluster in photosynthetic water-splitting enzyme. 4.6: Time-resolved structure of geminate states of myoglobin CO by X-ray absorption near-edge structure spectroscopy. 4.7: The structure-function relationship of the active sites in haemoprotein catalysis. 4.8: Soft X-ray absorption and X-ray magnetic dichroism in biology. Part 5: X-ray beamlines and detectors. 5.1: Synchrotron radiation sciences in Japan. 5.2: Diffraction and diffuse scattering beamlines for biophysical applications at the ESRF. 5.3: Developments in gas detectors for biophysics at the Daresbury SRS. 5.4: X-ray television detectors. 5.5: The development of X-ray television detectors at the Photon Factory. Part 6: Structural studies on muscle protein, muscle contraction, and filamentous virus. 6.1: What X-rays tell us about muscle contraction - then and now. 6.2: DNase I binding induces a conformational change in the actin monomer. 6.3: X-ray diffraction studies of activation and myosin head motions in frog sartorius muscle during isotonic and isometric contraction. 6.4: X-ray diffraction evidence for a specific actomyosin complex in live isometrically contracting frog sartorius muscle. 6.5: Modelling structural changes of the muscle thin filaments during an isometric contraction. 6.6: Synchrotron radiation in time-resolved X-ray diffraction studies of molecular movements in muscle. 6.7: Frequency dependence of the variation of the X-ray diffraction pattern from tetanized frog skeletal muscle during sinusoidal length changes. 6.8: X-ray diffraction experiments on various types of vertebrate muscle. 6.9: Application of synchrotron radiation to studies of the contractile apparatus of single intact muscle fibres. 6.10: Structural changes of crossbridges on contraction and relaxation induced by photolysis of caged ATP: an X-ray diffraction study at the Photon Factory. 6.11: Structural change of the myosin head detected by electron microscopy and small-angle X-ray scattering. 6.12: Electrostatic field around the actin filament. 6.13: X-ray diffraction studies of the thin filaments in a contracting molluscan smooth muscle. 6.14: Muscle diffraction at the Cornell High Energy Synchrotron Source. 6.15: Fibre diffraction studies on filamentous viruses. Part 7: X-ray microimaging. 7.1: Natural imaging of biological specimens with X-ray microscopes. 7.2: Soft X-ray microscopy at the National Synchrotron Light Source. 7.3: X-ray microscopy: present status and future prospects. 7.4: X-ray contact microscopy of human chromosome fibres. 7.5: Macromolecular transport in the zymogen granule measured by quantitative X-ray. 7.6: X-ray microscopy with multilayer mirrors: the MAXIMUM photoelectron microscope. 7.7: Application of the X-ray zooming tube to X-ray contact microscopy. 7.8: Hard X-ray scanning microscopy and micro X-ray absorption fine-structure spectroscopy studies on iron compounds in the enameloid of fish teeth. 7.9: The X-ray Microscopy Resource Center at the Advanced Light Source. Part 8: Medical applications of synchrotron radiation: angiography, computerized tomography, and others. 8.1: Synchrotron radiation coronary angiography in humans. 8.2: Digital subtraction angiography with synchrotron radiation in Russia. 8.3: A K-edge subtraction coronary angiography system using the dual linearly polarized synchrotron radiation beams from an ellipsoid multipole wiggler. 8.4: Coronary angiography at the Hamburger Synchrotronstrahlungslabor (HASYLAB). 8.5: Medical applications of synchrotron radiation at the National Synchrotron Light Source. Part 9: Radiation biophysics using synchrotron radiation. 9.1: Soft X-ray radiobiology and synchrotron radiation. 9.2: The use of synchrotron-produced ultrasoft X-rays to model radiobiological processes. 9.3: Radiation biology of inner cell ionization/excitation. 9.4: Radiation damage induced in free nucleotides and sulfur-containing amino acids by monoenergetic X-rays. 9.5: DNA damage induced by monochromatic photons from synchrotron radiation. 9.6: Ultraviolet free-electron laser facility at Brookhaven National Laboratory. 9.7: Biological effectiveness of low-energy electrons as revealed by synchrotron-produced soft X-rays. 9.8: Strand breaks in DNA in buffered solution induced by monochromatic X-rays around the K-shell absorption edge of phosphorus. 9.9: Action spectra for inactivation and mutagenesis of Bacillus subtilis spores in wavelength ranges between 0.1 and 300 nm

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