Sample Environment: Soft Matter Sample Environment for Small-Angle Neutron Scattering and Neutron Reflectometry

The FlexiProb project is a joint effort of three soft matter groups at the Universities of Bielefeld, Darmstadt, and Munich with scientific support from the European Spallation Source (ESS), the small-K advanced diffractometer (SKADI) beamline development group of the Jülich Centre for Neutron Science (JCNS), and the Heinz Maier-Leibnitz Zentrum (MLZ). Within this framework, a flexible and quickly interchangeable sample carrier system for small-angle neutron scattering (SANS) at the ESS was developed. In the present contribution, the development of a sample environment for the investigation of soft matter thin films with grazing-incidence small-angle neutron scattering (GISANS) is introduced. Therefore, components were assembled on an optical breadboard for the measurement of thin film samples under controlled ambient conditions, with adjustable temperature and humidity, as well as the optional in situ recording of the film thickness via spectral reflectance. Samples were placed in a 3D-printed spherical humidity metal chamber, which enabled the accurate control of experimental conditions via water-heated channels within its walls. A separately heated gas flow stream supplied an adjustable flow of dry or saturated solvent vapor. First test experiments proved the concept of the setup and respective component functionality.

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A temperature-controlled electric field sample environment for small-angle neutron scattering experiments

Review of Scientific Instruments ◽

10.1063/5.0040675 ◽

2021 ◽

Vol 92 (3) ◽

pp. 033903

Author(s):

Dominic W. Hayward ◽

Germinal Magro ◽

Anja Hörmann ◽

Sylvain Prévost ◽

Ralf Schweins ◽

...

Keyword(s):

Electric Field ◽

Neutron Scattering ◽

Small Angle ◽

Small Angle Neutron Scattering ◽

Field Sample ◽

Temperature Controlled ◽

Sample Environment

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Comment on “Cholesterol solubility limit in lipid membranes probed by small angle neutron scattering and MD simulations” by S. Garg et al., Soft Matter, 2014, 10, 9313

Soft Matter ◽

10.1039/c4sm02819h ◽

2015 ◽

Vol 11 (27) ◽

pp. 5580-5581

Author(s):

Richard M. Epand ◽

Diana Bach ◽

Ellen Wachtel

Keyword(s):

Phase Separation ◽

Neutron Scattering ◽

Small Angle ◽

Lipid Membranes ◽

Small Angle Neutron Scattering ◽

Soft Matter ◽

Md Simulations ◽

Solubility Limit ◽

Phospholipid Bilayers ◽

Cholesterol Solubility

As consistently described in the literature, the solubility limit of cholesterol in phospholipid bilayers is defined by its phase separation and crystallization.

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Neutron reflectometry and small-angle neutron scattering — Two complementary techniques for polymer blend investigations

Physica B Condensed Matter ◽

10.1016/s0921-4526(96)00959-3 ◽

1997 ◽

Vol 234-236 ◽

pp. 286-288 ◽

Cited By ~ 6

Author(s):

D.W. Schubert ◽

M. Stamm

Keyword(s):

Neutron Scattering ◽

Polymer Blend ◽

Small Angle ◽

Small Angle Neutron Scattering ◽

Neutron Reflectometry ◽

Complementary Techniques

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Soft Matter Sample Environments for Time-Resolved Small Angle Neutron Scattering Experiments: A Review

Applied Sciences ◽

10.3390/app11125566 ◽

2021 ◽

Vol 11 (12) ◽

pp. 5566

Author(s):

Volker S. Urban ◽

William T. Heller ◽

John Katsaras ◽

Wim Bras

Keyword(s):

Neutron Scattering ◽

Small Angle ◽

High Intensity ◽

Small Angle Neutron Scattering ◽

Soft Matter ◽

Condensed Matter ◽

Large Body ◽

Soft Condensed Matter ◽

Time Resolved ◽

Neutron Sources

With the promise of new, more powerful neutron sources in the future, the possibilities for time-resolved neutron scattering experiments will improve and are bound to gain in interest. While there is already a large body of work on the accurate control of temperature, pressure, and magnetic fields for static experiments, this field is less well developed for time-resolved experiments on soft condensed matter and biomaterials. We present here an overview of different sample environments and technique combinations that have been developed so far and which might inspire further developments so that one can take full advantage of both the existing facilities as well as the possibilities that future high intensity neutron sources will offer.

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Model Membranes and Their Interactions with Native and Artificial Lipoproteins

10.24834/isbn.9789178771325 ◽

2020 ◽

Author(s):

◽

Sarah Waldie

Keyword(s):

Neutron Scattering ◽

Small Angle ◽

Small Angle Neutron Scattering ◽

Model Membranes ◽

Neutron Reflectometry ◽

Model Systems ◽

High Density Lipoproteins ◽

The West ◽

Structural Characterisation ◽

Angle Scattering

Atherosclerosis arises from build-up of plaque in the blood, can result in cardiovascular disease and is the largest killer in the west. Low- and high-density lipoproteins are involved in the disease development by depositing and removing lipids to and from artery walls. These processes are complex and not fully understood however, therefore determining the specific roles of the components involved is of fundamental importance in the treatment of the disease. The work presented in this thesis investigates the production of recombinant tailor-deuterated cholesterol, the structure of cholesterol-containing model membranes and interactions of both native and reconstituted lipoproteins with model membranes. Deuteration is commonly used in neutron scattering for biological samples to provide highly important contrast and the complexity of the native lipoproteins leads to the use of more simple model systems where the compositions can be altered and investigated systematically. A protocol was developed to produce matchout-deuterated cholesterol for use in neutron scattering studies, as cholesterol is a hugely important component in membranes. The verification of the matchpoint of cholesterol was determined by small-angle neutron scattering and the localisation of cholesterol in model membranes was determined through the use of neutron reflectometry. The interactions of the native and reconstituted lipoproteins with model membranes were also followed by neutron reflectometry, while the structural characterisation of the reconstituted lipoproteins was carried out by small-angle scattering.

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X-ray space technology for focusing small-angle neutron scattering and neutron reflectometry

Physica B Condensed Matter ◽

10.1016/s0921-4526(00)00325-2 ◽

2000 ◽

Vol 283 (4) ◽

pp. 330-332 ◽

Cited By ~ 15

Author(s):

B. Alefeld ◽

L. Dohmen ◽

D. Richter ◽

Th. Brückel

Keyword(s):

Neutron Scattering ◽

Small Angle ◽

Small Angle Neutron Scattering ◽

Neutron Reflectometry ◽

Space Technology ◽

X Ray

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The basics of small-angle neutron scattering (SANS for new users of structural biology)

EPJ Web of Conferences ◽

10.1051/epjconf/202023603001 ◽

2020 ◽

Vol 236 ◽

pp. 03001

Author(s):

Cy M. Jeffries ◽

Zuzanna Pietras ◽

Dmitri I. Svergun

Keyword(s):

Neutron Scattering ◽

Structural Biology ◽

Small Angle ◽

Structural State ◽

Small Angle Neutron Scattering ◽

Soft Matter ◽

Higher Order ◽

Hydrogen Interaction ◽

The Way

Small-angle neutron scattering (SANS) provides a means to probe the time-preserved structural state(s) of bio-macromolecules in solution. As such, SANS affords the opportunity to assess the redistribution of mass, i.e., changes in conformation, which occur when macromolecules interact to form higher-order assemblies and to evaluate the structure and disposition of components within such systems. As a technique, SANS offers scope for ‘out of the box thinking’, from simply investigating the structures of macromolecules and their complexes through to where structural biology interfaces with soft-matter and nanotechnology. All of this simply rests on the way neutrons interact and scatter from atoms (largely hydrogens) and how this interaction differs from the scattering of neutrons from the nuclei of other ‘biological isotopes’. The following chapter describes the basics of neutron scattering for new users of structural biology in context of the neutron/hydrogen interaction and how this can be exploited to interrogate the structures of macromolecules, their complexes and nano-conjugates in solution.

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