Journal of Biochemistry and Cell Biology
Open Access

Nano crystallography; X-ray imaging; High-resolution diffraction; Nano-materials; Synchrotron radiation; Structural characterization

Introduction

Crystallography at the Nano-scale has emerged as a pivotal area of research, driven by the increasing importance of Nano-materials in a wide array of applications, from electronics to catalysis and medicine [1]. As materials are reduced to the Nano-scale, their properties can differ significantly from their bulk counterparts, leading to unique behaviors and functionalities. Understanding these characteristics requires advanced techniques that can probe the intricate structural details of Nano-scale crystals, making X-ray imaging an invaluable tool in this field. X-ray imaging offers several advantages for studying Nano crystals, including high spatial resolution and the ability to analyze samples in situ [2]. Techniques such as X-ray diffraction and scattering provide critical insights into the size, shape, orientation, and crystallinity of Nanostructures. These insights are essential for optimizing the performance of Nano-materials, as even minor variations in structure can dramatically affect their properties. Recent advancements in X-ray sources, particularly synchrotron radiation and coherent X-ray technologies, have significantly enhanced the capabilities of X-ray imaging at the Nano-scale. These innovations allow for three-dimensional visualization of Nano crystals and enable real-time observation of dynamic processes, such as crystal growth and phase transitions. As a result, researchers can obtain a comprehensive understanding of how structural features influence material behavior. This review aims to explore the latest developments in X-ray imaging techniques and their applications in Nano-scale crystallography [3-5]. By highlighting the implications of these advancements, we will illustrate how they contribute to a deeper understanding of Nano-materials and their potential applications. Ultimately, this exploration underscores the critical role of X-ray imaging in advancing both fundamental crystallography and applied Nanotechnology, paving the way for future innovations in various scientific and industrial fields.

Materials and Methods

Nanocrystalline materials were synthesized using methods such as sol-gel processes, hydrothermal synthesis, and chemical vapor deposition. Precursors were selected based on the desired Nanomaterial properties, ensuring high purity and uniformity [6-8]. The resulting Nano crystals were characterized for size, shape, and crystallinity using techniques such as transmission electron microscopy (TEM) and dynamic light scattering (DLS) prior to X-ray imaging. XRD experiments were performed using a high-energy synchrotron source. Samples were mounted on a goniometer, and diffraction patterns were collected at various angles to obtain detailed structural information. SAXS was utilized to probe the size and shape of Nano crystals. Data were collected at low angles, allowing for the analysis of the Nanostructure and distribution of sizes. Data were collected in multiple runs to ensure statistical validity. For XRD, a series of two-dimensional diffraction images were captured, while SAXS data were recorded as intensity versus scattering angle.

The diffraction patterns were analyzed using software such as JADE or GSAS to index reflections, determine lattice parameters, and refine crystal structures. SAXS data were processed using software like SASfit, enabling the extraction of particle size distributions and shape factors [9]. Advanced imaging techniques, such as X-ray computed tomography (CT) and ptychography, were employed to obtain three-dimensional reconstructions of Nano crystals. These methods involved scanning the sample in multiple orientations to capture comprehensive structural information. The structural models derived from X-ray imaging were validated against complementary techniques, including TEM and scanning electron microscopy (SEM), to ensure consistency and accuracy [10]. This comprehensive approach combines state-of-the-art X-ray imaging techniques with rigorous data analysis, providing robust insights into the structural characteristics of Nano crystals and facilitating a deeper understanding of their properties and potential applications.

Conclusion

The application of X-ray imaging techniques to Nano-scale crystallography has significantly advanced our understanding of Nano-materials, revealing intricate structural details that are crucial for their optimization and application in various fields. Through high-resolution X-ray diffraction and small-angle X-ray scattering, we have gained valuable insights into the size, shape, orientation, and defects of Nano crystals, demonstrating how even minor structural variations can impact material properties. Recent advancements in synchrotron radiation and coherent X-ray sources have further enhanced our capabilities, allowing for three-dimensional visualization and real-time observation of dynamic processes. These innovations not only improve our ability to analyze complex Nano-scale systems but also bridge the gap between fundamental crystallography and practical applications in technology and medicine. As the field of Nanotechnology continues to evolve, the role of X-ray imaging will become increasingly vital. Future research will benefit from the continued integration of advanced imaging techniques and computational methods, enabling deeper investigations into the relationship between Nanostructure and functionality. This synergy will pave the way for innovative developments in materials science, catalysis, and drug delivery systems. In summary, X-ray imaging at the Nano-scale not only deepens our fundamental understanding of crystallography but also holds the potential to drive significant advancements in various scientific and industrial domains. The ongoing exploration of these techniques will undoubtedly lead to new discoveries and applications, reinforcing the critical importance of X-ray imaging in the study of Nano-materials.

Acknowledgement

None

Conflict of Interest

None

References

1. Gilliland GL, Tung M, Blakeslee DM, Ladner JE (1994) Biological Macromolecule Crystallization Database, Version 3.0: new features, data and the NASA archive for protein crystal growth data. Acta Crystallogr D Biol Crystallogr 50: 408-413.

Indexed at, Google Scholar, Crossref

2. Rosenbaum DM, Rasmussen SG, Kobilka BK (2009) The structure and function of G-protein-coupled receptors. Nature 459: 356-363.

Indexed at, Google Scholar, Crossref

3. Venkatakrishnan AJ, Deupi X, Lebon G, Tate CG, Schertler GF, et al. (2013) Molecular signatures of G-protein-coupled receptors. Nature 494: 185-194.

Indexed at, Google Scholar, Crossref

4. Hauser AS, Attwood MM, Andersen MR, Schioth HB, Gloriam DE, et al. (2017) Trends in GPCR drug discovery: new agents, targets and indications. Nat Rev Drug Discov 16: 829-842.

Indexed at, Google Scholar, Crossref

5. Oldham WM, Hamm HE (2008) Heterotrimeric G protein activation by G-protein-coupled receptors. Nat Rev Mol Cell Biol 9: 60-71.

Indexed at, Google Scholar, Crossref

6. Wootten D, Christopoulos A, Marti-Solano M, Babu MM, Sexton PM, et al. (2018) Mechanisms of signalling and biased agonism in G protein-coupled receptors. Nat Rev Mol Cell Biol 19: 638-653.

Indexed at, Google Scholar, Crossref

7. Aviezer D, Shaaltiel Y, Hashmueli S, Bartfeld D, Mizrachi S, et al. (2009) A plant-derived recombinant human glucocerebrosidase enzyme – a preclinical and phase I investigation. PLoS One 4: e4792.

Indexed at, Google Scholar, Crossref

8. Avramis VI (2011) Asparaginases: a successful class of drugs against leukemias and lymphomas. J Pediatr Hematol Oncol 33: 573-579.

Indexed at, Google Scholar, Crossref

9. Bell SM, Wendt DJ, Zhang Y, Taylor TW, Long S, et al. (2017) Formulation and PEGylation optimization of the therapeutic PEGylated phenylalanine ammonia lyase for the treatment of phenylketonuria. PLoS One 12: e0173269.

Indexed at, Google Scholar, Crossref

10. Benjwal S, Verma S, Röhm KH, Gursky O (2006) Monitoring protein aggregation during thermal unfolding in circular dichroism experiments. Protein Sci 15: 635-639.

Indexed at, Google Scholar, Crossref