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Electron crystallographic analysis of two-dimensional streptavidin crystals coordinated to metal-chelated lipid monolayers

Academic Article
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Overview

authors

  • Frey, W.
  • Brink, J.
  • Schief, William
  • Chiu, W.
  • Vogel, V.

publication date

  • May 1998

journal

  • Biophysical Journal  Journal

abstract

  • Coordination of individual histidine residues located on a protein surface to metal-chelated lipid monolayers is a potentially general method for crystallizing proteins in two dimensions. It was shown recently by Brewster angle microscopy (BAM) that the model protein streptavidin binds via its surface histidines to Cu-DOIDA lipid monolayers, and aggregates into regularly shaped domains that have the appearance of crystals. We have used electron microscopy to confirm that the domains are indeed crystalline with lattice parameters similar to those of the same protein crystallized beneath biotinylated lipid monolayers. Although BAM demonstrates that the two-dimensional protein crystals grown via metal chelation are distinct from the biotin-bound crystals in both microscopic shape and thermodynamic behavior, the two crystal types show similar density projections and the same plane group symmetry.

subject areas

  • Adsorption
  • Biotin
  • Crystallography
  • Diglycerides
  • Histidine
  • Ligands
  • Microscopy
  • Microscopy, Electron
  • Organometallic Compounds
  • Protein Binding
  • Protein Conformation
  • Streptavidin
  • Thermodynamics
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Identity

PubMed Central ID

  • PMC1299607

International Standard Serial Number (ISSN)

  • 0006-3495

Digital Object Identifier (DOI)

  • 10.1016/S0006-3495(98)77973-1

PubMed ID

  • 9591691
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Additional Document Info

start page

  • 2674

end page

  • 2679

volume

  • 74

issue

  • 5

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