ArticleActa crystallographica. Section F, Structural biology and crystallization communications2006
Purification, crystallization and preliminary X-ray analysis of the outer membrane complex HasA-HasR from Serratia marcescens.
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 4 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
4 citing papers in PubMed.
- Structural basis of the signalling through a bacterial membrane receptor HasR deciphered by an integrative approach.The Biochemical journal · 2016Article
- Heme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complex.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Mutagenesis and molecular modeling reveal three key extracellular loops of the membrane receptor HasR that are involved in hemophore HasA binding.Journal of bacteriology · 2007Article
- Pyridine Hemochromagen Assay for Determining the Concentration of Heme in Purified Protein Solutions.Bio-protocolArticle
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Authors and funding
4 authors.
Funding
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Abstract
Serratia marcescens is able to acquire iron using its haem-acquisition system (;has'), which contains an outer membrane receptor HasR and a soluble haemophore HasA. After secretion, HasA binds free haem in the extracellular medium or extracts it from haemoproteins and delivers it to the receptor. Here, the crystallization of a HasA-HasR complex is reported. HasA and HasR have been overexpressed in Escherichia coli and the complex formed and crystallized. Small platelets and bunches of needles of dimensions 0.01 x 0.1 x 1 mm were obtained. A native data set has been collected to 6.8 A.
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