X-ray crystallography is a robust and powerful structural biology technique that provides high-resolution atomic structures of biomacromolecules. Scientists use this technique to unravel mechanistic and structural details of biological macromolecules (e.g., proteins, nucleic acids, protein complexes, protein-nucleic acid complexes, or large biological compartments). Since its inception, single-crystal cryocrystallography has never been performed in Türkiye due to the lack of a single-crystal X-ray diffractometer. The X-ray diffraction facility recently established at the University of Health Sciences, İstanbul, Türkiye will enable Turkish and international researchers to easily perform high-resolution structural analysis of biomacromolecules from single crystals. Here, we describe the technical and practical outlook of a state-of-the-art home-source X-ray, using lysozyme as a model protein. The methods and practice described in this article can be applied to any biological sample for structural studies. Therefore, this article will be a valuable practical guide from sample preparation to data analysis.
Yttrium-stabilized tetragonal zirconia polycrystalline (Y-TZP) ceramic is widely used as an all-ceramic core material because of its enhanced mechanical and aesthetic properties. The bond strength of Y-TZP restorations affects long-term success; hence, surface treatment is required on ceramic boundaries. This study evaluated the effect of different laser beam angles on Y-TZP-resin cement shear bond strength (SBS). Forty plates of Y-TZP ceramics were randomly assigned to four groups (n = 10). A femtosecond amplifier laser pulse was applied on Y-TZP surface with different incidence angles (90°, 75°, 60°, 45°). The resin cement was adhered onto the zirconia surfaces. The SBS of each sample was measured using universal testing machine at crosshead speed of 1 mm/min. The SBS was analyzed through one-way analysis of variance (ANOVA)/Tukey tests. The results showed that the degree of laser beam angle affects the SBS of resin cement to Y-TZP. The laser beam was applied to a surface with a 45° angle which resulted in significantly higher SBS (18.2 ± 1.43 MPa) than other groups (at 90° angulation (10.79 ± 1.8 MPa), at 75° (13.48 ± 1.2 MPa) and at 60° (15.85 ± 0.81 MPa); p < 0.001). This study shows that decreasing of the angle between the ceramic surface and the laser beam increased the SBS between the resin cement and the ceramic material, as well as the orifice.
X-ray crystallography is a robust and powerful structural biology technique that provides high-resolution atomic structures of biomacromolecules. Scientists use this technique to unravel mechanistic and structural details of biological macromolecules (e.g. proteins, nucleic acids, protein complexes, protein-nucleic acid complexes, or large biological compartments). Since its inception, single-crystal cryo-crystallography has never been performed in Turkiye due to the lack of a single-crystal X-ray diffractometer. The X-ray diffraction facility recently established at the University of Health Sciences, Istanbul, Turkiye will enable Turkish and international researchers to easily perform high-resolution structural analysis of biomacromolecules from single crystals. Here, we describe the technical and practical outlook of a state-of-the-art home-source X-ray, using lysozyme as a model protein. The methods and practice described in this article can be applied to any biological sample for structural studies. Therefore, this article will be a valuable practical guide from sample preparation to data analysis.
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