Structure of Protein Cage Supercrystals Revealed by Angular X‐ray Cross‐Correlation Analysis
Biohybrid supercrystals are highly ordered 3D assemblies of protein nanocages, offering versatile structural designs through the selection of protein nanocages and their ability to encapsulate various cargos within their cavities. By loading nanoparticles into these nanocages, diverse and complex su...
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| Format: | Article |
| Language: | English |
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Wiley-VCH
2025-08-01
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| Series: | Small Structures |
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| Online Access: | https://doi.org/10.1002/sstr.202400684 |
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| author | Kuan Hoon Ngoi Laurin Lang Young Yong Kim Niklas Mucke Gerard N. Hinsley Dongwon Kim Michael Rütten Lars Klemeyer Maximilian Ruffer Varnika Yadav Henrike Wagler Tobias Katenkamp Markus Perbandt Azat Khadiev Dmitri Novikov Tobias Beck Ivan A. Vartanyants |
| author_facet | Kuan Hoon Ngoi Laurin Lang Young Yong Kim Niklas Mucke Gerard N. Hinsley Dongwon Kim Michael Rütten Lars Klemeyer Maximilian Ruffer Varnika Yadav Henrike Wagler Tobias Katenkamp Markus Perbandt Azat Khadiev Dmitri Novikov Tobias Beck Ivan A. Vartanyants |
| author_sort | Kuan Hoon Ngoi |
| collection | DOAJ |
| description | Biohybrid supercrystals are highly ordered 3D assemblies of protein nanocages, offering versatile structural designs through the selection of protein nanocages and their ability to encapsulate various cargos within their cavities. By loading nanoparticles into these nanocages, diverse and complex superstructures can be engineered. In this study, individual biohybrid supercrystals are investigated using small‐angle X‐ray diffraction. As the samples may consist from single to several crystalline grains, angular X‐ray cross‐correlation analysis is used to analyze the angular correlations within 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, facilitating precise identification of the nanocage positions within the superlattice. The arrangement of nanoparticles in the unit cell is validated by comparing the experimental and calculated radial intensity profiles. The 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 capability of this technique for defect characterization and crystal engineering. |
| format | Article |
| id | doaj-art-fb55633b8d434c4c859af3b2cef504d7 |
| institution | Kabale University |
| issn | 2688-4062 |
| language | English |
| publishDate | 2025-08-01 |
| publisher | Wiley-VCH |
| record_format | Article |
| series | Small Structures |
| spelling | doaj-art-fb55633b8d434c4c859af3b2cef504d72025-08-20T03:59:25ZengWiley-VCHSmall Structures2688-40622025-08-0168n/an/a10.1002/sstr.202400684Structure of Protein Cage Supercrystals Revealed by Angular X‐ray Cross‐Correlation AnalysisKuan Hoon Ngoi0Laurin Lang1Young Yong Kim2Niklas Mucke3Gerard N. Hinsley4Dongwon Kim5Michael Rütten6Lars Klemeyer7Maximilian Ruffer8Varnika Yadav9Henrike Wagler10Tobias Katenkamp11Markus Perbandt12Azat Khadiev13Dmitri Novikov14Tobias Beck15Ivan A. Vartanyants16Photon Science, Deutsches Electronen‐Synchrotron DESY Deutsches Elektronen‐Synchrotron DESY Notkestr. 85 22607 Hamburg GermanyInstitute of Physical Chemistry Department of Chemistry University of Hamburg Grindelallee 117 20146 Hamburg GermanyBeamline DivisionPohang Accelerator Laboratory POSTECH Pohang 37673 Republic of KoreaInstitute of Physical Chemistry Department of Chemistry University of Hamburg Grindelallee 117 20146 Hamburg GermanyPhoton Science, Deutsches Electronen‐Synchrotron DESY Deutsches Elektronen‐Synchrotron DESY Notkestr. 85 22607 Hamburg GermanyBeamline DivisionPohang Accelerator Laboratory POSTECH Pohang 37673 Republic of KoreaInstitute of Physical Chemistry Department of Chemistry University of Hamburg Grindelallee 117 20146 Hamburg GermanyInstitute of Physical Chemistry Department of Chemistry University of Hamburg Grindelallee 117 20146 Hamburg GermanyInstitute of Physical Chemistry Department of Chemistry University of Hamburg Grindelallee 117 20146 Hamburg GermanyInstitute of Physical Chemistry Department of Chemistry University of Hamburg Grindelallee 117 20146 Hamburg GermanyInstitute of Physical Chemistry Department of Chemistry University of Hamburg Grindelallee 117 20146 Hamburg GermanyInstitute of Physical Chemistry Department of Chemistry University of Hamburg Grindelallee 117 20146 Hamburg GermanyInstitute of Physical Chemistry Department of Chemistry University of Hamburg Grindelallee 117 20146 Hamburg GermanyPhoton Science, Deutsches Electronen‐Synchrotron DESY Deutsches Elektronen‐Synchrotron DESY Notkestr. 85 22607 Hamburg GermanyPhoton Science, Deutsches Electronen‐Synchrotron DESY Deutsches Elektronen‐Synchrotron DESY Notkestr. 85 22607 Hamburg GermanyInstitute of Physical Chemistry Department of Chemistry University of Hamburg Grindelallee 117 20146 Hamburg GermanyPhoton Science, Deutsches Electronen‐Synchrotron DESY Deutsches Elektronen‐Synchrotron DESY Notkestr. 85 22607 Hamburg GermanyBiohybrid supercrystals are highly ordered 3D assemblies of protein nanocages, offering versatile structural designs through the selection of protein nanocages and their ability to encapsulate various cargos within their cavities. By loading nanoparticles into these nanocages, diverse and complex superstructures can be engineered. In this study, individual biohybrid supercrystals are investigated using small‐angle X‐ray diffraction. As the samples may consist from single to several crystalline grains, angular X‐ray cross‐correlation analysis is used to analyze the angular correlations within 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, facilitating precise identification of the nanocage positions within the superlattice. The arrangement of nanoparticles in the unit cell is validated by comparing the experimental and calculated radial intensity profiles. The 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 capability of this technique for defect characterization and crystal engineering.https://doi.org/10.1002/sstr.202400684angular X‐ray cross‐correlation analysisbiohybrid supercrystalsnanoparticles cargosprotein nanocages |
| spellingShingle | Kuan Hoon Ngoi Laurin Lang Young Yong Kim Niklas Mucke Gerard N. Hinsley Dongwon Kim Michael Rütten Lars Klemeyer Maximilian Ruffer Varnika Yadav Henrike Wagler Tobias Katenkamp Markus Perbandt Azat Khadiev Dmitri Novikov Tobias Beck Ivan A. Vartanyants Structure of Protein Cage Supercrystals Revealed by Angular X‐ray Cross‐Correlation Analysis Small Structures angular X‐ray cross‐correlation analysis biohybrid supercrystals nanoparticles cargos protein nanocages |
| title | Structure of Protein Cage Supercrystals Revealed by Angular X‐ray Cross‐Correlation Analysis |
| title_full | Structure of Protein Cage Supercrystals Revealed by Angular X‐ray Cross‐Correlation Analysis |
| title_fullStr | Structure of Protein Cage Supercrystals Revealed by Angular X‐ray Cross‐Correlation Analysis |
| title_full_unstemmed | Structure of Protein Cage Supercrystals Revealed by Angular X‐ray Cross‐Correlation Analysis |
| title_short | Structure of Protein Cage Supercrystals Revealed by Angular X‐ray Cross‐Correlation Analysis |
| title_sort | structure of protein cage supercrystals revealed by angular x ray cross correlation analysis |
| topic | angular X‐ray cross‐correlation analysis biohybrid supercrystals nanoparticles cargos protein nanocages |
| url | https://doi.org/10.1002/sstr.202400684 |
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