ArticleNature communications2021
Nucleation of protein mesocrystals via oriented attachment.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Navigating Classical and Nonclassical Realms of Nucleation and Crystallization.Small (Weinheim an der Bergstrasse, Germany) · 2026Review
- Quantitative Perspectives of Biomolecular Crystallization Thermodynamics.Advances in biochemical engineering/biotechnology · 2026Review
- Guanine Crystallization by Particle Attachment.Journal of the American Chemical Society · 2025Article
- Gypsum heterogenous nucleation pathways regulated by surface functional groups and hydrophobicity.Nature communications · 2025Article
- Unravelling complex mechanisms in materials processes with cryogenic electron microscopy.Chemical science · 2025Review
- Fusion crystallization reveals the behavior of both the 1TEL crystallization chaperone and the TNK1 UBA domain.Structure (London, England : 1993) · 2023Article
- Editorial: Recent advances and challenges in electron microscopy characterizations of radiation-sensitive nanoparticles.Frontiers in chemistry · 2023Article
- Unusual shape-preserved pathway of a core-shell phase transition triggered by orientational disorder.IUCrJ · 2023Article
- Crystallization of SrAlThe journal of physical chemistry. C, Nanomaterials and interfaces · 2022Article
- Nucleation of glucose isomerase protein crystals in a nonclassical disguise: The role of crystalline precursors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Self-assembly of proteins holds great promise for the bottom-up design and production of synthetic biomaterials. In conventional approaches, designer proteins are pre-programmed with specific recognition sites that drive the association process towards a desired organized state. Although proven effective, this approach poses restrictions on the complexity and material properties of the end-state. An alternative, hierarchical approach that has found wide adoption for inorganic systems, relies on the production of crystalline nanoparticles that become the building blocks of a next-level assembly process driven by oriented attachment (OA). As it stands, OA has not yet been observed for protein systems. Here we employ cryo-transmission electron microscopy (cryoEM) in the high nucleation rate limit of protein crystals and map the self-assembly route at molecular resolution. We observe the initial formation of facetted nanocrystals that merge lattices by means of OA alignment well before contact is made, satisfying non-trivial symmetry rules in the process. As these nanocrystalline assemblies grow larger we witness imperfect docking events leading to oriented aggregation into mesocrystalline assemblies. These observations highlight the underappreciated role of the interaction between crystalline nuclei, and the impact of OA on the crystallization process of proteins.
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Registered trials
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