Small-angle scattering and its interplay with crystallography, contrast variation in SAXS and SANS

Stuhrmann, H. B.

doi:10.1107/s0108767307046569

Cited by 36 publications

(15 citation statements)

References 74 publications

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“…This approach has largely been applied in (U)SANS experiments (cf. Stuhrmann and Kirste 1965;Stuhrmann 1974Stuhrmann , 2008Stuhrmann , 2012Ibel and Stuhrmann 1975;Stuhrmann et al 1976, Figure 29. Schematic illustration of contrast matching.…”

Section: Contrast Matchingmentioning

confidence: 96%

Characterization and Analysis of Porosity and Pore Structures

Anovitz

Cole

2015

Reviews in Mineralogy and Geochemistry

843

480

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Section: Contrast Matchingmentioning

confidence: 96%

Characterization and Analysis of Porosity and Pore Structures

Anovitz

Cole

2015

Reviews in Mineralogy and Geochemistry

843

480

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“…These techniques are useful for gaining information on the structural arrangement and dynamics of proteins as well as establishing correlations with stability in amorphous phases. Readers interested in other neutron techniques, or other applications of neutron scattering in biology, are referred to general reviews discussing the fundamentals of neutron scattering [15], [16], [17], [18], [19], neutron scattering for structural biology studies [13], [14], [20], [21], and contrast matching techniques for biological samples [22], [23], [24], [25].…”

Section: Introductionmentioning

confidence: 99%

Investigating Structure and Dynamics of Proteins in Amorphous Phases Using Neutron Scattering

Castellanos

McAuley

Curtis

2017

Computational and Structural Biotechnology Journal

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In order to increase shelf life and minimize aggregation during storage, many biotherapeutic drugs are formulated and stored as either frozen solutions or lyophilized powders. However, characterizing amorphous solids can be challenging with the commonly available set of biophysical measurements used for proteins in liquid solutions. Therefore, some questions remain regarding the structure of the active pharmaceutical ingredient during freezing and drying of the drug product and the molecular role of excipients. Neutron scattering is a powerful technique to study structure and dynamics of a variety of systems in both solid and liquid phases. Moreover, neutron scattering experiments can generally be correlated with theory and molecular simulations to analyze experimental data. In this article, we focus on the use of neutron techniques to address problems of biotechnological interest. We describe the use of small-angle neutron scattering to study the solution structure of biological molecules and the packing arrangement in amorphous phases, that is, frozen glasses and freeze-dried protein powders. In addition, we discuss the use of neutron spectroscopy to measure the dynamics of glassy systems at different time and length scales. Overall, we expect that the present article will guide and prompt the use of neutron scattering to provide unique insights on many of the outstanding questions in biotechnology.

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“…For cold neutrons, the coherent scattering length of an ensemble of spins of a single isotope does not depend on Q (Stuhrmann 2004(Stuhrmann , 2008 …”

mentioning

confidence: 99%

Combining structure and dynamics: non-denaturing high-pressure effect on lysozyme in solution

Ortore

Spinozzi

Mariani

et al. 2009

J. R. Soc. Interface.

130

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Small-angle X-ray scattering (SAXS) and elastic and quasi-elastic neutron scattering techniques were used to investigate the high-pressure-induced changes on interactions, the low-resolution structure and the dynamics of lysozyme in solution. SAXS data, analysed using a global-fit procedure based on a new approach for hydrated protein form factor description, indicate that lysozyme completely maintains its globular structure up to 1500 bar, but significant modifications in the protein -protein interaction potential occur at approximately 600-1000 bar. Moreover, the mass density of the protein hydration water shows a clear discontinuity within this pressure range. Neutron scattering experiments indicate that the global and the local lysozyme dynamics change at a similar threshold pressure. A clear evolution of the internal protein dynamics from diffusing to more localized motions has also been probed. Protein structure and dynamics results have then been discussed in the context of protein -water interface and hydration water dynamics. According to SAXS results, the new configuration of water in the first hydration layer induced by pressure is suggested to be at the origin of the observed local mobility changes.

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Small-angle scattering and its interplay with crystallography, contrast variation in SAXS and SANS

Cited by 36 publications

References 74 publications

Characterization and Analysis of Porosity and Pore Structures

Characterization and Analysis of Porosity and Pore Structures

Investigating Structure and Dynamics of Proteins in Amorphous Phases Using Neutron Scattering

Combining structure and dynamics: non-denaturing high-pressure effect on lysozyme in solution

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