ArticleJournal of bacteriology2010
Analysis of the intact surface layer of Caulobacter crescentus by cryo-electron tomography.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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Who cites it
17 citing papers in PubMed, 35 citations in OpenAlex.
- Assembly, architecture and functional roles of microbial surface layers.Nature reviews. Microbiology · 2026Review
- An N4-likeJournal of bacteriology · 2026Article
- An N4-likebioRxiv : the preprint server for biology · 2025Article
- Engineering High-Yield Biopolymer Secretion Creates an Extracellular Protein Matrix for Living Materials.mSystems · 2021Article
- Preparing samples from whole cells using focused-ion-beam milling for cryo-electron tomography.Nature protocols · 2020Article
- Topologically-guided continuous protein crystallization controls bacterial surface layer self-assembly.Nature communications · 2019Article
- Article
- Engineering the S-Layer of Caulobacter crescentus as a Foundation for Stable, High-Density, 2D Living Materials.ACS synthetic biology · 2019Article
- Environmental Calcium Controls Alternate Physical States of the Caulobacter Surface Layer.Biophysical journal · 2017Article
- Structure of the hexagonal surface layer on Caulobacter crescentus cells.Nature microbiology · 2017Article
- Two Outer Membrane Proteins Contribute to Caulobacter crescentus Cellular Fitness by Preventing Intracellular S-Layer Protein Accumulation.Applied and environmental microbiology · 2016Article
- Surface-layer protein from Caulobacter crescentus: expression, purification and X-ray crystallographic analysis.Acta crystallographica. Section F, Structural biology communications · 2016Article
- A new view into prokaryotic cell biology from electron cryotomography.Nature reviews. Microbiology · 2016Review
- Bioadsorption of Rare Earth Elements through Cell Surface Display of Lanthanide Binding Tags.Environmental science & technology · 2016Article
- Global and Targeted Lipid Analysis of Gemmata obscuriglobus Reveals the Presence of Lipopolysaccharide, a Signature of the Classical Gram-Negative Outer Membrane.Journal of bacteriology · 2016Article
- Small-molecule labeling of live cell surfaces for three-dimensional super-resolution microscopy.Journal of the American Chemical Society · 2014Article
- Structural studies of planctomycete Gemmata obscuriglobus support cell compartmentalisation in a bacterium.PloS one · 2014Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The surface layers (S layers) of those bacteria and archaea that elaborate these crystalline structures have been studied for 40 years. However, most structural analysis has been based on electron microscopy of negatively stained S-layer fragments separated from cells, which can introduce staining artifacts and allow rearrangement of structures prone to self-assemble. We present a quantitative analysis of the structure and organization of the S layer on intact growing cells of the Gram-negative bacterium Caulobacter crescentus using cryo-electron tomography (CET) and statistical image processing. Instead of the expected long-range order, we observed different regions with hexagonally organized subunits exhibiting short-range order and a broad distribution of periodicities. Also, areas of stacked double layers were found, and these increased in extent when the S-layer protein (RsaA) expression level was elevated by addition of multiple rsaA copies. Finally, we combined high-resolution amino acid residue-specific Nanogold labeling and subtomogram averaging of CET volumes to improve our understanding of the correlation between the linear protein sequence and the structure at the 2-nm level of resolution that is presently available. The results support the view that the U-shaped RsaA monomer predicted from negative-stain tomography proceeds from the N terminus at one vertex, corresponding to the axis of 3-fold symmetry, to the C terminus at the opposite vertex, which forms the prominent 6-fold symmetry axis. Such information will help future efforts to analyze subunit interactions and guide selection of internal sites for display of heterologous protein segments.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.