ArticleProceedings of the National Academy of Sciences of the United States of America2022
Nucleation of glucose isomerase protein crystals in a nonclassical disguise: The role of crystalline precursors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Crystallisation triggered by mass diffusion at a lower local supersaturation.Communications chemistry · 2026Article
- Engineered hybrid cell membrane nanosystems for treating cardiovascular diseases.Materials today. Bio · 2025Review
- A generic cross-seeding approach to protein crystallization.Journal of applied crystallography · 2025Article
- Supramolecular Synthons in Protein-Ligand Frameworks.Crystal growth & design · 2024Article
- Protein nanocondensates: the next frontier.Biophysical reviews · 2023Review
- Editorial: Recent advances and challenges in electron microscopy characterizations of radiation-sensitive nanoparticles.Frontiers in chemistry · 2023Article
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Authors and funding
4 authors.
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Abstract
Protein crystallization is an astounding feat of nature. Even though proteins are large, anisotropic molecules with complex, heterogeneous surfaces, they can spontaneously group into two- and three-dimensional arrays with high precision. And yet, the biggest hurdle in this assembly process, the formation of a nucleus, is still poorly understood. In recent years, the two-step nucleation model has emerged as the consensus on the subject, but it still awaits extensive experimental verification. Here, we set out to reconstruct the nucleation pathway of the candidate protein glucose isomerase (GI), for which there have been indications that it may follow a two-step nucleation pathway under certain conditions. We find that the precursor phase present during the early stages of the reaction process is nanoscopic crystallites that have lattice symmetry equivalent to the mature crystals found at the end of a crystallization experiment. Our observations underscore the need for experimental data at a lattice-resolving resolution on other proteins so that a general picture of protein crystal nucleation can be formed.
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