ArticleActa crystallographica. Section F, Structural biology and crystallization communications2008
There is a baby in the bath water: AcrB contamination is a major problem in membrane-protein crystallization.
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 22 papers.
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Who cites it
22 citing papers in PubMed, 45 citations in OpenAlex.
- Assembly and inhibition of transferable TMexCD1-TOprJ1 efflux pump.Nature communications · 2025Article
- Off-target structural insights: ArnA and AcrB in bacterial membrane-protein cryo-EM analysis.Acta crystallographica. Section D, Structural biology · 2025Article
- Insights into substrate recognition and export tunnel preferences in the efflux transporter AcrB.Protein science : a publication of the Protein Society · 2025Article
- Structural Insights into Transporter-Mediated Drug Resistance in Infectious Diseases.Journal of molecular biology · 2021Review
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- Changes in Membrane Protein Structural Biology.Biology · 2020Review
- Detecting the nature and solving the crystal structure of a contaminant protein from an opportunistic pathogen.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Crystal structure of the Escherichia coli transcription termination factor Rho.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Be Cautious with Crystal Structures of Membrane Proteins or Complexes Prepared in Detergents.Crystals · 2020Article
- Membrane Protein Production and Purification from Escherichia coli and Sf9 Insect Cells.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Structure of the dihydrolipoamide succinyltransferase catalytic domain from Escherichia coli in a novel crystal form: a tale of a common protein crystallization contaminant.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Shaping the lipid composition of bacterial membranes for membrane protein production.Microbial cell factories · 2019Article
- BpeB, a major resistance-nodulation-cell division transporter from Burkholderia cenocepacia: construct design, crystallization and preliminary structural analysis.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Expression, purification, and contaminant detection for structural studies of Ralstonia metallidurance ClC protein rm1.PloS one · 2017Article
- Article
- An overview of heavy-atom derivatization of protein crystals.Acta crystallographica. Section D, Structural biology · 2016Review
- Large-scale identification of membrane proteins with properties favorable for crystallization.Protein science : a publication of the Protein Society · 2015Article
- Stubborn contaminants: influence of detergents on the purity of the multidrug ABC transporter BmrA.PloS one · 2014Article
- Article
- Triosephosphate isomerase is a common crystallization contaminant of soluble His-tagged proteins produced in Escherichia coli.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the course of a crystallographic study of the Methanosarcina mazei CorA transporter, the membrane protein was obtained with at least 95% purity and was submitted to crystallization trials. Small crystals (<100 microm) were grown that diffracted to 3.42 A resolution and belonged to space group R32, with unit-cell parameters a = b = 145.74, c = 514.0 A. After molecular-replacement attempts using available CorA structures as search models failed to yield a solution, it was discovered that the crystals consisted of an Escherichia coli contaminating protein, acriflavine resistance protein B (AcrB), that was present at less than 5% in the protein preparations. AcrB contamination is a major problem when expressing membrane proteins in E. coli since it binds naturally to immobilized metal-ion affinity chromatography (IMAC) resins. Here, the structure is compared with previously deposited AcrB structures and strategies are proposed to avoid this contamination.
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