ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009
Expression, purification and preliminary X-ray analysis of the Neisseria meningitidis outer membrane protein PorB.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Broad Stability and pH-Mediated Reversible Disassembly of In Vitro Assembled Bacterial Microcompartment Shells.Nano letters · 2026Article
- An antibiotic-resistance conferring mutation in a neisserial porin: Structure, ion flux, and ampicillin binding.Biochimica et biophysica acta. Biomembranes · 2021Article
- Crystallographic analysis of Neisseria meningitidis PorB extracellular loops potentially implicated in TLR2 recognition.Journal of structural biology · 2014Article
- The biology of Neisseria adhesins.Biology · 2013Article
- The amino acid sequence of Neisseria lactamica PorB surface-exposed loops influences Toll-like receptor 2-dependent cell activation.Infection and immunity · 2012Article
- Human airway epithelial cell responses to Neisseria lactamica and purified porin via Toll-like receptor 2-dependent signaling.Infection and immunity · 2010Article
- Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The Neisseria meningitidis outer membrane protein PorB was expressed in Escherichia coli and purified from inclusion bodies by denaturation in urea followed by refolding in buffered LDAO on a size-exclusion column. PorB has been crystallized in three different crystal forms: C222, R32 and P6(3). The C222 crystal form may contain either one or two PorB monomers in the asymmetric unit, while both the R32 and P6(3) crystal forms contained one PorB monomer in the asymmetric unit. Of the three, the P6(3) crystal form had the best diffraction quality, yielding data extending to 2.3 A resolution.
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Registered trials
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