Structural Biology Using Electrons and X-rays: An Introduction for Biologists


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Diffraction Techniques in Structural Biology.

As second-generation machines were optimised to produce brighter beams, a fundamental limit was approaching. To meet the increasing demands of a growing synchrotron user community, a new approach was required: insertion devices. Insertion devices are arrays of magnets placed into the straight sections of the storage ring, which could be retro-fitted to second-generation machines and were quickly incorporated into existing synchrotrons.

Insertion devices help to create a beam that is very bright and with intensity peaks with a wavelength that can be varied by adjusting the field strength often the gap between two magnet arrays. The increased brightness made data collection faster, and tunable wavelengths benefited crystallographers and spectroscopists alike. By the early s machines were being designed with insertion devices in place from the start, and the first such third-generation source, the European Synchrotron Radiation Facility ESRF in Grenoble, France, started operating in There are now more than 50 dedicated light sources in the world, combining both second- and third-generation machines, which cover a wide spectral range from infrared to hard X-rays.

The experimental configurations of different synchrotron facilities are quite similar. The storage rings where the light is generated have many ports, which each open onto a beamline, where scientists set up their experiments and collect data. The beamlines, however, can vary a lot in the details depending on the experimental methods they are used for.

It represents the largest single UK science investment for 40 years and will have the capacity to host 40 beamlines. The Diamond Light Source supports a huge range of scientific disciplines, including condensed matter physics, chemistry, nanophysics, structural biology, engineering, environmental science and cultural heritage. Seven Nobel Prizes in Physics have been awarded for X-ray related work. For example, British physicists Sir William Henry Bragg and William Lawrence Bragg shared the prize for using X-ray diffraction as a technique to determine crystal structure.

Synchrotron facilities have had a positive and significant impact on many areas. In , the Nobel Prize in Chemistry was awarded to Prof. Roger Kornberg for his synchrotron-based research into how genes copy themselves, a process involved in many human diseases and stem-cell treatment. Similarly, more than companies have benefited from construction or technology contracts for the Diamond Light Source and a quarter of the science carried out at the ESRF links directly to industry.

The demand for synchrotron light has meant that third-generation machines are being built around the world, and existing machines continue to be developed to provide brighter X-rays, increased user hours and more flexible experimental stations. The modular nature of modern synchrotrons means that new technologies can be incorporated into existing machines as they arrive.

By using powerful linear accelerator technology, fourth-generation sources — known as free-electron lasers FELs — can generate shorter, femtosecond pulses but with the same intensity in each peak as synchrotron sources emit in one second, producing X-rays that are millions of times brighter in each pulse than the most powerful synchrotrons. The Institute is a charity registered in England and Wales no. Institute of Physics publications Publications: Publications: Publications: Publications: Publications: Publications: Publications: Publications: Publications: Publications: Publications: Publications: Publications: Archive.

Synchrotron light Synchrotron light is used today to carry out fundamental research in areas as diverse as condensed matter physics, pharmaceutical research and cultural heritage. What is synchrotron light? Roessle, M. Time-resolved small angle scattering: kinetics and structural data from proteins in solution.

Jacques, D. Small-angle scattering for structural biology--expanding the frontier while avoiding the pitfalls. Protein Sci. Grishaev, A. Sample preparation, data collection and preliminary data analysis in biomolecular solution X-ray scattering.

Glatter, O. Feigin, L.

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Publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution. Acta Crystallogr. D68 , — Cardiac myosin-binding protein C decorates F-actin: implications for cardiac function. USA , — Lakey, J.

Blob-ology and biology of cryo-EM: an interview with Helen Saibil

Neutrons for biologists: a beginner's guide, or why you should consider using neutrons. Zaccai, G. SANS provides unique information on the structure and function of biological macromolecules in solution. Physica B , — Heller, W. Small-angle neutron scattering for molecular biology: basics and instrumentation. Krueger, J. Small-angle scattering studies of biological macromolecules in solution. Jacrot, B. Determination of molecular weight by neutron scattering. Biopolymers 20 , — Sears, V. Neutron scattering lengths and cross sections.

Neutron News 3 , 26—37 MULCh: modules for the analysis of small-angle neutron contrast variation data from biomolecular assemblies. Konarev, P. A posteriori determination of the useful data range for small-angle scattering experiments on dilute monodisperse systems. Lafleur, J. Automated microfluidic sample-preparation platform for high-throughput structural investigation of proteins by small-angle X-ray scattering.

Skou, M. Bertani, G. Studies on lysogenesis. The mode of phage liberation by lysogenic Escherichia coli. Kuwamoto, S. Radiation damage to a protein solution, detected by synchrotron X-ray small-angle scattering: dose-related considerations and suppression by cryoprotectants.

Jeffries, C. Folta-Stogniew, E. Determination of molecular masses of proteins in solution: implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory. Structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis and insights into its solution state. D Biol. Corrections to scaling in the hydrodynamic properties of dilute polymer solutions. Brewer, A. Characterizing the size, shape, and compactness of a polydisperse prolate ellipsoidal particle via quadruple-detector hydrodynamic chromatography.

Analyst , — Rubinson, K. Small-angle neutron scattering and the errors in protein structures that arise from uncorrected background and intermolecular interactions. Trewhella, J.

X-ray crystallography

Structure 21 , — Bradford, M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Gasteiger, E. Protein identification and analysis tools on the ExPASy server. Walker, J. Cleland,, W.

Dithiothreitol, a new protective reagent for sh groups. Biochemistry 3 , — Stevens, R. The stabilities of various thiol compounds used in protein purifications. Coordination properties of Tris 2-carboxyethyl phosphine, a newly introduced thiol reductant, and its oxide. Krezel, A. Coordination of heavy metals by dithiothreitol, a commonly used thiol group protectant.

Han, J. A procedure for quantitative determination of Tris 2-Carboxyethyl phosphine, an odorless reducing agent more stable and effective than dithiothreitol. Zhao, H. On the distribution of protein refractive index increments. Guinier, A.

Helical Translations – A blog about biochemistry and structural biology

Determination of the regularization parameter in indirect-transform methods using perceptual criteria. A new method for the evaluation of small-angle scattering data. Mylonas, E. Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering. Krigbaum, W.

Molecular conformation of egg-white lysozyme and bovine alpha-lactalbumin in solution. Biochemistry 9 , — Watson, M. Probing the average local structure of biomolecules using small-angle scattering and scaling laws. Fischer, H. Determination of the molecular weight of proteins in solution from a single small-angle X-ray scattering measurement on a relative scale. Accurate assessment of mass, models and resolution by small-angle scattering. Nature , — Fritz, G. SAXS instruments with slit collimation: investigation of resolution and flux. Voss, N.

Orthaber, D. SAXS experiments on absolute scale with Kratky systems using water as a secondary standard. Wignall, G. Absolute calibration of small-angle neutron scattering data. Protein hydration in solution: experimental observation by x-ray and neutron scattering.

USA 95 , — Leiting, B. Predictable deuteration of recombinant proteins expressed in Escherichia coli. Goryunov, A. Sheu, S. Molecular dynamics of hydrogen bonds in protein-D2O: the solvent isotope effect.


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A , — Baghurst, P. The effect of D 2 O on the association of -lactoglobulin A.


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  • Dougan, L. A single-molecule perspective on the role of solvent hydrogen bonds in protein folding and chemical reactions.

    Chemphyschem 9 , — Tehei, M. Fast dynamics of halophilic malate dehydrogenase and BSA measured by neutron scattering under various solvent conditions influencing protein stability. USA 98 , — Jasnin, M. Solvent isotope effect on macromolecular dynamics in E. Automated pipeline for purification, biophysical and x-ray analysis of biomacromolecular solutions.

    Glasoe, P. Use of glass electrodes to measure acidities in deuterium oxide. Oxford University Press, Wood, K. Exploring the structure of biological macromolecules in solution using Quokka, the small angle neutron scattering instrument, at ANSTO. A , 44—51 Mokbel, N. K7del is a common TPM2 gene mutation associated with nemaline myopathy and raised myofibre calcium sensitivity.

    Brain , — Mathew, E. Liquid-chromatography-coupled SAXS for accurate sizing of aggregating proteins. David, G.

    Structural Biology Using Electrons and X-rays: An Introduction for Biologists Structural Biology Using Electrons and X-rays: An Introduction for Biologists
    Structural Biology Using Electrons and X-rays: An Introduction for Biologists Structural Biology Using Electrons and X-rays: An Introduction for Biologists
    Structural Biology Using Electrons and X-rays: An Introduction for Biologists Structural Biology Using Electrons and X-rays: An Introduction for Biologists
    Structural Biology Using Electrons and X-rays: An Introduction for Biologists Structural Biology Using Electrons and X-rays: An Introduction for Biologists
    Structural Biology Using Electrons and X-rays: An Introduction for Biologists Structural Biology Using Electrons and X-rays: An Introduction for Biologists
    Structural Biology Using Electrons and X-rays: An Introduction for Biologists Structural Biology Using Electrons and X-rays: An Introduction for Biologists

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