Amphiphiles modify the properties of detergent solutions used in crystallization of membrane proteins

M. A. Rosenow, J. C. Williams, James Paul Allen

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

The effect of the amphiphile heptanetriol on the properties of solutions containing several detergents commonly used for crystallization of membrane proteins was characterized. The critical micelle concentration was found to be relatively unchanged by the presence of the amphiphile. In contrast, the addition of heptanetriol to solutions containing both detergent and polyethylene glycol exhibited significant shifts in the clouding behavior, with the largest shifts being for lauryl dimethylamine oxide. These results suggest that conditions favorable for crystallization of integral membrane proteins can be inferred from the properties of the detergents and amphiphiles.

Original languageEnglish
Pages (from-to)925-927
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume57
Issue number6
DOIs
Publication statusPublished - 2001

Fingerprint

Amphiphiles
detergents
Crystallization
Detergents
Membrane Proteins
crystallization
membranes
proteins
Critical micelle concentration
shift
Micelles
Oxides
glycols
polyethylenes
micelles
oxides

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

Cite this

Amphiphiles modify the properties of detergent solutions used in crystallization of membrane proteins. / Rosenow, M. A.; Williams, J. C.; Allen, James Paul.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 57, No. 6, 2001, p. 925-927.

Research output: Contribution to journalArticle

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