ArticleActa crystallographica. Section F, Structural biology and crystallization communications2008
Crystallization and preliminary X-ray analysis of CrgA, a LysR-type transcriptional regulator from pathogenic Neisseria meningitidis MC58.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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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
8 citing papers in PubMed, 13 citations in OpenAlex.
- CrgA Protein Represses AlkB2 Monooxygenase and Regulates the Degradation of Medium-to-Long-ChainFrontiers in microbiology · 2019Article
- Article
- Efficient production and purification of recombinant murine kindlin-3 from insect cells for biophysical studies.Journal of visualized experiments : JoVE · 2014Article
- Isolation and characterization of mutant Sinorhizobium meliloti NodD1 proteins with altered responses to luteolin.Journal of bacteriology · 2013Article
- A plate-based high-throughput assay for virus stability and vaccine formulation.Journal of virological methods · 2012Article
- Structure of the regulatory domain of the LysR family regulator NMB2055 (MetR-like protein) from Neisseria meningitidis.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- The structure of a reduced form of OxyR from Neisseria meningitidis.BMC structural biology · 2010Article
- The structure of CrgA from Neisseria meningitidis reveals a new octameric assembly state for LysR transcriptional regulators.Nucleic acids research · 2009Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Although LysR-type regulators (LTTRs) represent the largest family of transcriptional regulators in bacteria, the full-length structure of only one annotated LTTR (CbnR) has been deposited in the PDB. CrgA, a LTTR from pathogenic Neisseria meningitidis MC58, which is up-regulated upon bacterial cell contact with human epithelial cells, has been cloned, purified and crystallized. Crystals of full-length CrgA were obtained after buffer screening with a thermal shift assay and concentration with 0.2 M NDSB-256. Data were collected from two crystal forms of full-length CrgA belonging to space groups P2(1)2(1)2(1) and P2(1), diffracting to 3.0 and 3.8 A resolution and consistent with the presence of between six and ten and between ten and 20 copies of CrgA in the asymmetric unit, respectively. In addition, diffraction data were collected to 2.3 A resolution from the selenomethionine derivative of the regulatory domain of CrgA. The crystals belonged to space group P2(1) and contained two molecules in the asymmetric unit.
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