Home > Publications database > Structure of Protein Cage Supercrystals revealed by Angular X-ray Cross-Correlation Analysis > print |
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100 | 1 | _ | |a Ngoi, Kuan Hoon |0 P:(DE-H253)PIP1102996 |b 0 |
245 | _ | _ | |a Structure of Protein Cage Supercrystals revealed by Angular X-ray Cross-Correlation Analysis |
260 | _ | _ | |a Weinheim |c 2025 |b Wiley-VCH |
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520 | _ | _ | |a Biohybrid supercrystals are highly ordered three-dimensional (3D) assemblies of protein nanocages, offering versatile structural designs through their ability to encapsulate various inorganic nanoparticles. By loading nanoparticles into these nanocages, diverse and complex superstructures can be engineered. In this study, we investigate individual biohybrid supercrystals using small angle X-ray diffraction (SAXD). We employ Angular X-ray Cross-Correlation Analysis (AXCCA) to the intensity distribution in 3D reciprocal space, enabling the determination of the unit cell parameters of the superlattice. Encapsulated nanoparticles serve as effective X-ray scattering markers, enabling precise localization of protein nanocages within the superlattice. The arrangement of nanoparticles in the unit cell is validated by comparing the experimental and calculated radial intensity profile. Our findings confirm the superlattice structures of unitary protein-nanoparticle composites, binary composites (including homobinary and heterobinary designs), and supercrystals with core-shell morphologies. Furthermore, single-grain and twin-domain structures are identified, demonstrating the potential of this technique for defect characterization and crystal engineering. |
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700 | 1 | _ | |a Beck, Tobias |0 P:(DE-H253)PIP1090581 |b 13 |e Corresponding author |
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