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Crystals
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Small and Wide Angle X-ray Scattering Applied to Nano- and...
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Small and Wide Angle X-ray Scattering Applied to Nano- and Biomaterials

A special issue of Crystals (ISSN 2073-4352). This special issue belongs to the section "Inorganic Crystalline Materials".

Deadline for manuscript submissions: closed (31 December 2020) | Viewed by 22229

Special Issue Editors

Dr. Dritan Siliqi

E-Mail Website
Guest Editor
Institute of Crystallography- CNR, Via G. Amendola, 122/O, 70126 Bari, Italy
Interests: protein crystallography; small and wide angle X-ray scattering (SAXS and WAXS); BioSAXS; biological molecules; rare diseases; phasing algorithm; nano- and bio-materials; X-ray imaging
Special Issues, Collections and Topics in MDPI journals
Dr. Francesco Scattarella

E-Mail Website
Co-Guest Editor
Institute of Crystallography- CNR, Via G. Amendola, 122/O 70126 Bari, Italy
Interests: small and wide angle X-ray scattering (SAXS and WAXS) and GISAXS applied to nanomaterials; medical image analysis; electron microscopy; software developing for SWAXS/GISAXS/EM data analysis

Special Issue Information

Dear Colleagues,

Small- and wide- angle X-ray scattering (SAXS/WAXS) are powerful experimental techniques widely used in several fields of materials science. Both these techniques enable the characterization of nanoscale and molecular structures in a variety of materials, such as biomacromolecules, liquid nanoparticle dispersions/colloids, nanocomposites, polymers, fiber-like materials, surfactants, microemulsions, liquid crystals, mesoporous materials, etc.

We invite researchers to contribute to this Special Issue, which is intended to serve as a unique multidisciplinary forum covering broad aspects on both techniques applied to nano and bio-materials. Contributions on methods and software devoted to SAXS and WAXS data analysis are welcomed as well.

The potential topics include but are not limited to:

  • SAXS applied to macromolecules to deal the protein complexes;
  • Application on several fiber-like materials for different applications, ranging from medicine to technology;
  • Methods and computer software packages for SAXS/WAXS data analysis (new or improvements of the previous ones).

Dr. Dritan Siliqi
Dr. Francesco Scattarella
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Crystals is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2100 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • SAXS and WAXS
  • Colloidal nanoparticles
  • Biomolecules
  • Collagen-tissue engineering
  • Fiber-like materials
  • Computer software

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Published Papers (4 papers)

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Research

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13 pages, 4912 KiB  
Article
Structural Analysis of the Partially Disordered Protein EspK from Mycobacterium Tuberculosis
by Abril Gijsbers, Nuria Sánchez-Puig, Ye Gao, Peter J. Peters, Raimond B. G. Ravelli and Dritan Siliqi
Crystals 2021, 11(1), 18; https://doi.org/10.3390/cryst11010018 - 28 Dec 2020
Cited by 4 | Viewed by 3909
Abstract
For centuries, tuberculosis has been a worldwide burden for human health, and gaps in our understanding of its pathogenesis have hampered the development of new treatments. ESX-1 is a complex machinery responsible for the secretion of virulence factors that manipulate the host response. [...] Read more.
For centuries, tuberculosis has been a worldwide burden for human health, and gaps in our understanding of its pathogenesis have hampered the development of new treatments. ESX-1 is a complex machinery responsible for the secretion of virulence factors that manipulate the host response. Despite the importance of these secreted proteins for pathogenicity, only a few of them have been structurally and functionally characterised. Here, we describe a structural study of the ESX-secretion associated protein K (EspK), a 74 kDa protein known to be essential for the secretion of other substrates and the cytolytic effects of ESX-1. Small-Angle X-ray Scattering (SAXS) data show that EspK is a long molecule with a maximal dimension of 228 Å. It consists of two independent folded regions at each end of the protein connected by a flexible unstructured region driving the protein to coexist as an ensemble of conformations. Limited proteolysis identified a 26 kDa globular domain at the C-terminus of the protein consisting of a mixture of α-helices and β-strands, as shown by circular dichroism (CD) and SAXS. In contrast, the N-terminal portion is mainly helical with an elongated shape. Sequence conservation suggests that this architecture is preserved amongst the different mycobacteria species, proposing specific roles for the N- and C-terminal domains assisted by the middle flexible linker. Full article
(This article belongs to the Special Issue Small and Wide Angle X-ray Scattering Applied to Nano- and Biomaterials)
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18 pages, 3184 KiB  
Article
Adding Size Exclusion Chromatography (SEC) and Light Scattering (LS) Devices to Obtain High-Quality Small Angle X-Ray Scattering (SAXS) Data
by Melissa A. Graewert, Stefano Da Vela, Tobias W. Gräwert, Dmitry S. Molodenskiy, Clément E. Blanchet, Dmitri I. Svergun and Cy M. Jeffries
Crystals 2020, 10(11), 975; https://doi.org/10.3390/cryst10110975 - 27 Oct 2020
Cited by 42 | Viewed by 6411
Abstract
We describe the updated size-exclusion chromatography small angle X-ray scattering (SEC-SAXS) set-up used at the P12 bioSAXS beam line of the European Molecular Biology Laboratory (EMBL) at the PETRAIII synchrotron, DESY Hamburg (Germany). The addition of size exclusion chromatography (SEC) directly on-line to [...] Read more.
We describe the updated size-exclusion chromatography small angle X-ray scattering (SEC-SAXS) set-up used at the P12 bioSAXS beam line of the European Molecular Biology Laboratory (EMBL) at the PETRAIII synchrotron, DESY Hamburg (Germany). The addition of size exclusion chromatography (SEC) directly on-line to the SAXS capillary has become a well-established approach to reduce the effects of the sample heterogeneity on the SAXS measurements. The additional use of multi-angle laser light scattering (MALLS), UV absorption spectroscopy, refractive index (RI), and quasi-elastic light scattering (QELS) in parallel to the SAXS measurements enables independent molecular weight validation and hydrodynamic radius estimates. This allows one to address sample monodispersity as well as conformational heterogeneity. The benefits of the current SEC-SAXS set-up are demonstrated on a set of selected standard proteins. The processed SEC-SAXS data and models are provided in the Small Angle Scattering Biological Data Bank (SASBDB) and are labeled as “bench-marked” datasets that include the unsubtracted data frames spanning the respective SEC elution profiles and corresponding MALLS-UV-RI-QELS data. These entries provide method developers with datasets suitable for testing purposes, in addition to an educational resource for SAS data analysis and modeling. Full article
(This article belongs to the Special Issue Small and Wide Angle X-ray Scattering Applied to Nano- and Biomaterials)
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15 pages, 13740 KiB  
Article
Effect of Cholesterol and Ibuprofen on DMPC-β-Aescin Bicelles: A Temperature-Dependent Wide-Angle X-ray Scattering Study
by Ramsia Geisler, Sylvain Prévost, Rajeev Dattani and Thomas Hellweg
Crystals 2020, 10(5), 401; https://doi.org/10.3390/cryst10050401 - 16 May 2020
Cited by 10 | Viewed by 4240
Abstract
β -aescin is a versatile biosurfactant extracted from the seeds of the horse chestnut tree Aesculus hippocastanum with anti-cancer potential and is commonly used in the food and pharmaceutical and cosmetic industries. In this article, wide-angle X-ray scattering (WAXS) is used in order [...] Read more.
β -aescin is a versatile biosurfactant extracted from the seeds of the horse chestnut tree Aesculus hippocastanum with anti-cancer potential and is commonly used in the food and pharmaceutical and cosmetic industries. In this article, wide-angle X-ray scattering (WAXS) is used in order to study the modifications of the structural parameters at the molecular scale of lipid bilayers in the form of bicelles composed of 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) and the triterpenoid saponin β -aescin. In particular, the impact on the cooperative phase transition and the structural parameters of the DMPC bilayers at different compositions and temperatures is of special interest. Moreover, we show how cholesterol and the non-steroidal anti-inflammatory drug (NSAID) ibuprofen modulate the structural parameters of the β -aescin-DMPC assemblies on a molecular scale. Ibuprofen and cholesterol interact with different parts of the bilayer, namely the head-region in the former and the tail-region in the latter case allowing for specific molecular packing and phase formation in the binary and ternary mixtures. Full article
(This article belongs to the Special Issue Small and Wide Angle X-ray Scattering Applied to Nano- and Biomaterials)
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Review

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13 pages, 1667 KiB  
Review
Wide Angle X-Ray Scattering to Study the Atomic Structure of Polymeric Fibers
by Teresa Sibillano, Alberta Terzi, Liberato De Caro, Massimo Ladisa, Davide Altamura, Anna Moliterni, Rocco Lassandro, Francesco Scattarella, Dritan Siliqi and Cinzia Giannini
Crystals 2020, 10(4), 274; https://doi.org/10.3390/cryst10040274 - 4 Apr 2020
Cited by 10 | Viewed by 6568
Abstract
Natural fibrillar-like macromolecules find applications in several fields, thanks to their peculiar features, and are considered perfect building blocks for natural and artificial functional materials. Indeed, fibrous proteins (such as collagen or fibroin) are commonly used in scaffold fabrication for biomedical applications, due [...] Read more.
Natural fibrillar-like macromolecules find applications in several fields, thanks to their peculiar features, and are considered perfect building blocks for natural and artificial functional materials. Indeed, fibrous proteins (such as collagen or fibroin) are commonly used in scaffold fabrication for biomedical applications, due to the high biophysical similarity with the extracellular matrix (ECM) which stimulates tissue regeneration. In the textile industry, cellulose-based fabrics are widely used in place of cotton and viscose, which both have sustainability issues related to their fabrication. With this in mind, the structural characterization of the materials at molecular scale plays a fundamental role in gaining insight into the fiber assembly process. In this work, we report on three fibers of research interest (i.e., type I collagen, silk fibroin extracted from Bombyx mori, and cellulose) to show the power of wide-angle X-ray scattering to characterize both intra- and intermolecular parameters of fibrous polymers. The latest possibilities offered in the X-ray scattering field allow one to study fibers at solid state or dispersed in solutions as well as to perform quantitative scanning X-ray microscopy of tissues entirely or partially made by fibers. Full article
(This article belongs to the Special Issue Small and Wide Angle X-ray Scattering Applied to Nano- and Biomaterials)
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