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Rational design of lipid for membrane protein crystallization

Academic Article
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Overview

authors

  • Misquitta, Y.
  • Cherezov, Vadim
  • Havas, F.
  • Patterson, S.
  • Mohan, J. M.
  • Wells, A. J.
  • Hart, D. J.
  • Caffrey, M.

publication date

  • 2004

journal

  • Journal of Structural Biology  Journal

abstract

  • The lipidic cubic phase has been used to grow crystals of membrane proteins for high-resolution structure determination. However, the original, so-called, in meso method does not work reliably at low temperatures, where proteins are generally more stable, because the hosting lipid turns solid. The need existed therefore for a lipid that forms the cubic phase and that supports crystal growth at low temperatures. We created a database of phase diagrams and used it to design such a lipid. X-ray diffraction showed that the new lipid exhibits designed phase behavior. Further, it produces diffraction quality membrane protein crystals by the in meso method at 6 degrees C. This demonstrates that lipidic materials, like their protein counterparts are amenable to rational design. The same approach as used in this study should find application in extending the range of membrane proteins crystallizable by the in meso method and in tailoring transport of cubic phases for controlled delivery and uptake.

subject areas

  • Carbon
  • Crystallization
  • Crystallography, X-Ray
  • Glycerol
  • Halobacterium salinarum
  • Lipids
  • Membrane Proteins
  • Protein Conformation
  • Temperature
  • Water
  • X-Ray Diffraction
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Research

keywords

  • X-ray diffraction
  • cubic phase
  • monoacylglycerol
  • phase diagram
  • structure
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Identity

International Standard Serial Number (ISSN)

  • 1047-8477

Digital Object Identifier (DOI)

  • 10.1016/j.jsb.2004.06.008

PubMed ID

  • 15477097
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Additional Document Info

start page

  • 169

end page

  • 175

volume

  • 148

issue

  • 2

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