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231226s2023 xx |||||o 00| ||eng c |
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|a 10.1002/adma.202212065
|2 doi
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|a pubmed25n1180.xml
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|a (NLM)36932732
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Ferlez, Bryan H
|e verfasserin
|4 aut
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|a Heterologous Assembly of Pleomorphic Bacterial Microcompartment Shell Architectures Spanning the Nano- to Microscale
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|c 2023
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 09.06.2023
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|a Date Revised 03.06.2024
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © 2023 The Authors. Advanced Materials published by Wiley-VCH GmbH.
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|a Many bacteria use protein-based organelles known as bacterial microcompartments (BMCs) to organize and sequester sequential enzymatic reactions. Regardless of their specialized metabolic function, all BMCs are delimited by a shell made of multiple structurally redundant, yet functionally diverse, hexameric (BMC-H), pseudohexameric/trimeric (BMC-T), or pentameric (BMC-P) shell protein paralogs. When expressed without their native cargo, shell proteins have been shown to self-assemble into 2D sheets, open-ended nanotubes, and closed shells of ≈40 nm diameter that are being developed as scaffolds and nanocontainers for applications in biotechnology. Here, by leveraging a strategy for affinity-based purification, it is demonstrated that a wide range of empty synthetic shells, many differing in end-cap structures, can be derived from a glycyl radical enzyme-associated microcompartment. The range of pleomorphic shells observed, which span ≈2 orders of magnitude in size from ≈25 nm to ≈1.8 µm, reveal the remarkable plasticity of BMC-based biomaterials. In addition, new capped nanotube and nanocone morphologies are observed that are consistent with a multicomponent geometric model in which architectural principles are shared among asymmetric carbon, viral protein, and BMC-based structures
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|a Journal Article
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|a bacterial microcompartments
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4 |
|a fullerenes
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4 |
|a nanocones
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4 |
|a nanotubes
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|a self-assembly
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|a synthetic biology
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|a Bacterial Proteins
|2 NLM
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| 700 |
1 |
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|a Kirst, Henning
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Greber, Basil J
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Nogales, Eva
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Sutter, Markus
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Kerfeld, Cheryl A
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Advanced materials (Deerfield Beach, Fla.)
|d 1998
|g 35(2023), 23 vom: 15. Juni, Seite e2212065
|w (DE-627)NLM098206397
|x 1521-4095
|7 nnas
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| 773 |
1 |
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|g volume:35
|g year:2023
|g number:23
|g day:15
|g month:06
|g pages:e2212065
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| 856 |
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|u http://dx.doi.org/10.1002/adma.202212065
|3 Volltext
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