ArticleProceedings of the National Academy of Sciences of the United States of America2010
Self-catalyzed growth of S layers via an amorphous-to-crystalline transition limited by folding kinetics.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed.
- Gluebodies Offer a Route To Improve Crystal Reliability and Diversity through Transferable Nanobody Mutations That Introduce Constitutive Close Contacts.ACS central science · 2025Article
- Manipulating the Assembly and Architecture of Fibrillar Silk.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Assembly and Functionality of 2D Protein Arrays.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Two-dimensional silk.Science advances · 2024Article
- Article
- Shape-Anisotropic Assembly of Protein Nanocages with Identical Building Blocks by Designed Intermolecular π-π Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- In vitro investigation of protein assembly by combined microscopy and infrared spectroscopy at the nanometer scale.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Accounting for the Presence of Molecular Clusters in Modeling and Interpreting Nucleation and Growth.Crystal growth & design · 2022Article
- Encoding hierarchical assembly pathways of proteins with DNA.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Protein interface redesign facilitates the transformation of nanocage building blocks to 1D and 2D nanomaterials.Nature communications · 2021Article
- Nucleation of protein mesocrystals via oriented attachment.Nature communications · 2021Article
- A New Method for Dispersing Pristine Carbon Nanotubes Using Regularly Arranged S-Layer Proteins.Nanomaterials (Basel, Switzerland) · 2021Article
- Molecular Logic of Prokaryotic Surface Layer Structures.Trends in microbiology · 2021Review
- S-Layer Ultrafiltration Membranes.Membranes · 2021Review
- Controlled and Stable Patterning of Diverse Inorganic Nanocrystals on Crystalline Two-Dimensional Protein Arrays.Biochemistry · 2021Article
- LytR-CpsA-Psr Glycopolymer Transferases: Essential Bricks in Gram-Positive Bacterial Cell Wall Assembly.International journal of molecular sciences · 2021Review
- Hierarchical supramolecular assembly of a single peptoid polymer into a planar nanobrush with two distinct molecular packing motifs.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Article
- A bacterial surface layer protein exploits multistep crystallization for rapid self-assembly.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The importance of nonclassical, multistage crystallization pathways is increasingly evident from theoretical studies on colloidal systems and experimental investigations of proteins and biomineral phases. Although theoretical predictions suggest that proteins follow these pathways as a result of fluctuations that create unstable dense-liquid states, microscopic studies indicate these states are long-lived. Using in situ atomic force microscopy to follow 2D assembly of S-layer proteins on supported lipid bilayers, we have obtained a molecular-scale picture of multistage protein crystallization that reveals the importance of conformational transformations in directing the pathway of assembly. We find that monomers with an extended conformation first form a mobile adsorbed phase, from which they condense into amorphous clusters. These clusters undergo a phase transition through S-layer folding into crystalline clusters composed of compact tetramers. Growth then proceeds by formation of new tetramers exclusively at cluster edges, implying tetramer formation is autocatalytic. Analysis of the growth kinetics leads to a quantitative model in which tetramer creation is rate limiting. However, the estimated barrier is much smaller than expected for folding of isolated S-layer proteins, suggesting an energetic rationale for this multistage pathway.
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