ArticleActa crystallographica. Section F, Structural biology and crystallization communications2006
Expression, crystallization and preliminary X-ray crystallographic studies of the outer membrane protein OmpW from Escherichia coli.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 37 citations in OpenAlex.
- From Environmental Organism to Nosocomial Threat:Antibiotics (Basel, Switzerland) · 2026Review
- Carbapenem-ResistantAntibiotics (Basel, Switzerland) · 2026Review
- Outer Membrane Porins Contribute to Antimicrobial Resistance in Gram-Negative Bacteria.Microorganisms · 2023Review
- Properties and Phylogeny of 76 Families of Bacterial and Eukaryotic Organellar Outer Membrane Pore-Forming Proteins.PloS one · 2016Article
- The Borrelia afzelii outer membrane protein BAPKO_0422 binds human factor-H and is predicted to form a membrane-spanning β-barrel.Bioscience reports · 2015Article
- Article
- Comparative investigation of the genomic regions involved in antigenic variation of the TprK antigen among treponemal species, subspecies, and strains.Journal of bacteriology · 2012Article
- Hypochlorous acid and hydrogen peroxide-induced negative regulation of Salmonella enterica serovar Typhimurium ompW by the response regulator ArcA.BMC microbiology · 2012Article
- Comprehensive analyses of transport proteins encoded within the genome of "Aromatoleum aromaticum" strain EbN1.The Journal of membrane biology · 2009Article
- Structure and function of colicin S4, a colicin with a duplicated receptor-binding domain.The Journal of biological chemistry · 2009Article
- Expression, crystallization and preliminary X-ray analysis of an outer membrane protein from Thermus thermophilus HB27.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
OmpW is an eight-stranded 21 kDa molecular-weight beta-barrel protein from the outer membrane of Gram-negative bacteria. It is a major antigen in bacterial infections and has implications in antibiotic resistance and in the oxidative degradation of organic compounds. OmpW from Escherichia coli was cloned and the protein was expressed in inclusion bodies. A method for refolding and purification was developed which yields properly folded protein according to circular-dichroism measurements. The protein has been crystallized and crystals were obtained that diffracted to a resolution limit of 3.5 angstroms. The crystals belong to space group P422, with unit-cell parameters a = 122.5, c = 105.7 angstroms. A homology model of OmpW is presented based on known structures of eight-stranded beta-barrels, intended for use in molecular-replacement trials.
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