Download PDF by J. Fitter: Neutron Scattering in Biology

Contents

* Neutron Scattering for Biology T.A. Harroun, G.D. Wignall, J. KatsarasPart I Elastic Techniques * unmarried Crystal Neutron Diffraction and Protein Crystallography, C.C. Wilson, D.A. Myles
* Neutron Protein Crystallography: Hydrogen and Hydration in Proteins,N. Niimura
* Neutron Protein Crystallography: Technical elements and a few Case reports at present functions and past, M. Blakeley, A.J.K. Gilboa, J. Habash, J.R. Helliwell, D. Myles, J. Raftery
* Detergent Binding in Membrane Protein Crystals by way of Neutron Crystallography, P. Timmins
* High-Angle Neutron Fiber Diffraction within the research of organic structures, V.T. Forsyth, I.M. Parrot
* Neutron Scattering from Biomaterials in advanced pattern Environments, J. Katsaras, T.A. Harroun, M.P. Nieh, M. Chakrapani, M.J. Watson, V.A. Raghunathan
* Small-Angle Neutron Scattering from organic Molecules, J.K. Krueger, G.D. Wignall .
* Small perspective Neutron Scattering from Proteins, Nucleic Acids, and Viruses, S. Krueger, U.A. Perez-Salas, S.K. Gregurick, D. Kuzmanovic
* constitution and Kinetics of Proteins saw by way of Small attitude Neutron Scattering, M.W. Roessle, R.P. May
* advanced organic buildings: Collagen and Bone, P. Fratzl, O. Paris
* Structural Investigations of Membranes in Biology by way of Neutron Reflectometry, C.F. Majkrzak, N.F. Berk, S. Krueger, U.A. Perez-Salas Protein Adsorption and Interactions at Interfaces, J.R. Lu
* complicated Biomimetic constructions at Fluid Surfaces and Solid-Liquid Interfaces, T. Gutberlet, M. LЂoschePart II Inelastic Techniques * Quasielastic Neutron Scattering in Biology, R.E. Lechner, S. Longeville .
* Quasielastic Neutron Scattering in Biology, half II: purposes, R.E. Lechner, S. Longeville .
* Conformational Dynamics Measured with Proteins in answer, J. more fit .
* referring to Protein Dynamics to operate and constitution: The red Membrane, U. Lehnert, M. Weik
* Biomolecular Spectroscopy utilizing Pulsed-Source tools, H.D. Middendorf
* Brownian Oscillator research of Molecular Motions in Biomolecules, W. Doster .
* inner Dynamics of Proteins and DNA: Analogy to Glass-Forming platforms, A.P. Sokolov, R.B. Gregory .
* constitution and Dynamics of version Membrane platforms Probed via Elastic and Inelastic Neutron Scattering, T. Salditt, M.C. RheinstЂadter
* Subnanosecond Dynamics of Proteins in resolution: MD Simulations and Inelastic Neutron Scattering, M. Tarek, D.J. Tobias

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The major limitation on the signal-to-noise ratio in neutron diffraction from biological (as well as all other hydrogenous materials) is that hydrogen has a large incoherent neutron scattering factor of 80 barns that produces a high level background that significantly reduces the signal to noise ratio of the diffraction data. The corresponding value for the deuterium isotope is ∼2 barns; isotopic substitution of deuterium for hydrogen therefore results in huge reductions in the incoherent scattering background and order of magnitude improvement in signal to noise.

In general, when solving a crystal structure from diffraction data one has to deal with the well-known phase problem. This problem arises from the fact that the structure factor is a complex function, however, the complex part, or the phase, is lost in the measured intensity. A technique devised to resolve the phase problem is isomorphous replacement, and involves the addition of an element which effectively changes the neutron or electron density contrast of the crystal. In X-ray crystallography, this usually means the incorporation of heavy atoms such as, Hg into the structure.

Wilson et al. His-219: DD1 NE2 ND1 His-53: DD1 DD2 NE2 ND1 Fig. 3. Preliminary density maps from glucose isomerase, measured on PCS at LANSCE (left). 6 ˚ A 2Fo -Fc positive nuclear density in blue and the negative nuclear density in red for the side chain of Tyrosine 10 in W3Y rubredoxin (Pf). An example map from neutron data collected at cryogenic temperature 15 K on LADI at the ILL (right) beamline, promises to deliver a further order of magnitude improvement in performance for neuron protein crystallography.

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