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Crystallography of the integral membrane protein emre from escherichia coli

Academic Article
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Overview

authors

  • Ma, C.
  • Chang, Geoffrey

publication date

  • December 2004

journal

  • Acta Crystallographica Section D-Biological Crystallography  Journal

abstract

  • Crystals of the EmrE membrane-protein imposed several technical challenges for X-ray crystallography, including high mosaicity, poor diffraction and a relatively large number of heavy atoms. Consequently, the heavy-atom substructure solution was difficult to obtain. By removing the histidine tag for protein purification, the mosaicity and the diffraction quality were greatly improved. The direct-methods Shake-and-Bake program SnB was successful in locating the heavy-atom sites from a mutant of EmrE which lacks a cysteine and therefore has a reduction in the number of heavy-atom sites. The substructure solution was solved from data with anomalous difference at a resolution of 5.5 A and the structure was determined to 3.8 A.

subject areas

  • Antiporters
  • Crystallography, X-Ray
  • Cysteine
  • Drug Resistance, Multiple
  • Escherichia coli
  • Escherichia coli Proteins
  • Histidine
  • Membrane Proteins
  • Models, Molecular
  • Mutation
  • Polymerase Chain Reaction
  • Protein Conformation
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Identity

International Standard Serial Number (ISSN)

  • 0907-4449

Digital Object Identifier (DOI)

  • 10.1107/s090744490402548x

PubMed ID

  • 15583400
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Additional Document Info

start page

  • 2399

end page

  • 2402

volume

  • 60

issue

  • Pt 12 No 2

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