A putative siderophore-interacting protein from the marine bacterium Shewanella frigidimarina NCIMB 400: Cloning, expression, purification, crystallization and X-ray diffraction analysis

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Abstract

Siderophore-binding proteins (SIPs) perform a key role in iron acquisition in multiple organisms. In the genome of the marine bacterium Shewanella frigidimarina NCIMB 400, the gene tagged as SFRI-RS12295 encodes a protein from this family. Here, the cloning, expression, purification and crystallization of this protein are reported, together with its preliminary X-ray crystallographic analysis to 1.35 Å resolution. The SIP crystals belonged to the monoclinic space group P21, with unit-cell parameters a = 48.04, b = 78.31, c = 67.71 Å, α = 90, β = 99.94, γ = 90°, and are predicted to contain two molecules per asymmetric unit. Structure determination by molecular replacement and the use of previously determined ∼2 Å resolution SIP structures with ∼30% sequence identity as templates are ongoing.

Original languageEnglish
Pages (from-to)667-671
Number of pages5
JournalActa Crystallographica Section F:Structural Biology Communications
Volume72
DOIs
Publication statusPublished - 1 Sep 2016

Keywords

  • crystallographic analysis
  • Shewanella frigidimarina
  • siderophore-interacting protein

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