Bio-SANS—A dedicated facility for neutron structural biology at Oak Ridge National Laboratory

Lynn, Gary W.; Heller, William T.; Urban, Volker S.; Wígnall, G. D.; Weiss, Kevin L.; Myles, Dean A. A.

doi:10.1016/j.physb.2006.05.133

Cited by 68 publications

(51 citation statements)

References 5 publications

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“…SANS Measurements-SANS measurements were performed using the Center for Structural Molecular Biology Bio-SANS instrument at the High Flux Isotope Reactor of Oak Ridge National Laboratory (26). The wavelength was 6.0 Å, and the wavelength spread, ⌬/, was set to 0.14.…”

Section: Methodsmentioning

confidence: 99%

Small Angle Neutron Scattering Reveals pH-dependent Conformational Changes in Trichoderma reesei Cellobiohydrolase I

Pingali

O’Neill

McGaughey

et al. 2011

Journal of Biological Chemistry

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Cellobiohydrolase I (Cel7A) of the fungus Trichoderma reesei (now classified as an anamorph of Hypocrea jecorina) hydrolyzes crystalline cellulose to soluble sugars, making it of key interest for producing fermentable sugars from biomass for biofuel production. The activity of the enzyme is pH-dependent, with its highest activity occurring at pH 4 -5. To probe the response of the solution structure of Cel7A to changes in pH, we measured small angle neutron scattering of it in a series of solutions having pH values of 7.0, 6.0, 5.3, and 4.2. As the pH decreases from 7.0 to 5.3, the enzyme structure remains well defined, possessing a spatial differentiation between the cellulose binding domain and the catalytic core that only changes subtly. At pH 4.2, the solution conformation of the enzyme changes to a structure that is intermediate between a properly folded enzyme and a denatured, unfolded state, yet the secondary structure of the enzyme is essentially unaltered. The results indicate that at the pH of optimal activity, the catalytic core of the enzyme adopts a structure in which the compact packing typical of a fully folded polypeptide chain is disrupted and suggest that the increased range of structures afforded by this disordered state plays an important role in the increased activity of Cel7A through conformational selection.

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Section: Methodsmentioning

confidence: 99%

Small Angle Neutron Scattering Reveals pH-dependent Conformational Changes in Trichoderma reesei Cellobiohydrolase I

Pingali

O’Neill

McGaughey

et al. 2011

Journal of Biological Chemistry

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“…The SANS experiments were performed using the Bio-SANS (CG3) of the high-flux isotope reactor of the Oak Ridge National Laboratory (29). Samples were measured at room temperature in sealed, 1-mm-pathlength quartz cuvettes at concentrations of ϳ500 g/ml for BHK and ϳ400 g/ml for C7-10 samples.…”

Section: Growth Of Virusmentioning

confidence: 99%

The Structure of Sindbis Virus Produced from Vertebrate and Invertebrate Hosts as Determined by Small-Angle Neutron Scattering

Piper

Meilleur

et al. 2010

J Virol

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The complex natural cycle of vectored viruses that transition between host species, such as between insects and mammals, makes understanding the full life cycle of the virus an incredibly complex problem. Sindbis virus, an arbovirus and prototypic alphavirus having an inner protein shell and an outer glycoprotein coat separated by a lipid membrane, is one example of a vectored virus that transitions between vertebrate and insect hosts. While evidence of host-specific differences in Sindbis virus has been observed, no work has been performed to characterize the impact of the host species on the structure of the virus. Here, we report the first study of the structural differences between Sindbis viruses grown in mammalian and insect cells, which were determined by small-angle neutron scattering (SANS), a nondestructive technique that did not decrease the infectivity of the Sindbis virus particles studied. The scattering data and modeling showed that, while the radial position of the lipid bilayer did not change significantly, it was possible to conclude that it did have significantly more cholesterol when the virus was grown in mammalian cells. Additionally, the outer protein coat was found to be more extended in the mammalian Sindbis virus. The SANS data also demonstrated that the RNA and nucleocapsid protein share a closer interaction in the mammalian-cell-grown virus than in the virus from insect cells.

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“…The temperature was set at 25 ± 0.1°C. Further information on the instrumentation is available elsewhere [22]. A droplet (h-oil/h-surfactant/D 2 O) deuteration contrast scheme was used to obtain structural information.…”

Section: Phase Diagramsmentioning

confidence: 99%

Characterization of Microemulsion Systems Formed by a Mixed 1,3‐Dioxolane Ethoxylate/Octyl Glucoside Surfactant System

Alkhatib

Hayes

Urban

2009

J Surfact & Detergents

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Bio-SANS—A dedicated facility for neutron structural biology at Oak Ridge National Laboratory

Cited by 68 publications

References 5 publications

Small Angle Neutron Scattering Reveals pH-dependent Conformational Changes in Trichoderma reesei Cellobiohydrolase I

Small Angle Neutron Scattering Reveals pH-dependent Conformational Changes in Trichoderma reesei Cellobiohydrolase I

The Structure of Sindbis Virus Produced from Vertebrate and Invertebrate Hosts as Determined by Small-Angle Neutron Scattering

Characterization of Microemulsion Systems Formed by a Mixed 1,3‐Dioxolane Ethoxylate/Octyl Glucoside Surfactant System

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