The influence of detergents and amphiphiles on the solubility of the light-harvesting I complex

M. A. Rosenow, D. Brune, James Paul Allen

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The effect of detergents and amphiphiles on protein solubility and their use in crystallization solutions was examined for an integral membrane protein, the light-harvesting I complex from Rhodospirillum centenum. Measurement by a centrifugation assay of the solubility of the protein in different detergents and amphiphiles showed high protein-solubility values when either octyl glucoside or lauryldimethylamine-N-oxide was present with heptanetriol or when deoxycholate was present with spermine. The detergent/amphiphile combinations that resulted in high protein solubility were shown to be successful for crystallization of the protein, suggesting that crystallization is favored for detergents and amphiphiles that optimize the solubility of integral membrane proteins. The amphiphiles effective for crystallization were found using laser mass spectrometry to displace the lauryldimethylamine-N-oxide bound to the protein. These results suggest that mass spectrometry can be used for screening of favorable crystallization conditions.

Original languageEnglish
Pages (from-to)1422-1428
Number of pages7
JournalActa Crystallographica Section D: Biological Crystallography
Volume59
Issue number8
DOIs
Publication statusPublished - Aug 1 2003

Fingerprint

Amphiphiles
detergents
Detergents
Solubility
Crystallization
solubility
proteins
Light
crystallization
Proteins
Rhodospirillum centenum
Oxides
Mass spectrometry
Mass Spectrometry
Membrane Proteins
Deoxycholic Acid
mass spectroscopy
Spermine
Centrifugation
membranes

ASJC Scopus subject areas

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

Cite this

The influence of detergents and amphiphiles on the solubility of the light-harvesting I complex. / Rosenow, M. A.; Brune, D.; Allen, James Paul.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 59, No. 8, 01.08.2003, p. 1422-1428.

Research output: Contribution to journalArticle

@article{c95c10a932f944dc9c1214a9f73030a3,
title = "The influence of detergents and amphiphiles on the solubility of the light-harvesting I complex",
abstract = "The effect of detergents and amphiphiles on protein solubility and their use in crystallization solutions was examined for an integral membrane protein, the light-harvesting I complex from Rhodospirillum centenum. Measurement by a centrifugation assay of the solubility of the protein in different detergents and amphiphiles showed high protein-solubility values when either octyl glucoside or lauryldimethylamine-N-oxide was present with heptanetriol or when deoxycholate was present with spermine. The detergent/amphiphile combinations that resulted in high protein solubility were shown to be successful for crystallization of the protein, suggesting that crystallization is favored for detergents and amphiphiles that optimize the solubility of integral membrane proteins. The amphiphiles effective for crystallization were found using laser mass spectrometry to displace the lauryldimethylamine-N-oxide bound to the protein. These results suggest that mass spectrometry can be used for screening of favorable crystallization conditions.",
author = "Rosenow, {M. A.} and D. Brune and Allen, {James Paul}",
year = "2003",
month = "8",
day = "1",
doi = "10.1107/S0907444903011909",
language = "English",
volume = "59",
pages = "1422--1428",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "0907-4449",
publisher = "John Wiley and Sons Inc.",
number = "8",

}

TY - JOUR

T1 - The influence of detergents and amphiphiles on the solubility of the light-harvesting I complex

AU - Rosenow, M. A.

AU - Brune, D.

AU - Allen, James Paul

PY - 2003/8/1

Y1 - 2003/8/1

N2 - The effect of detergents and amphiphiles on protein solubility and their use in crystallization solutions was examined for an integral membrane protein, the light-harvesting I complex from Rhodospirillum centenum. Measurement by a centrifugation assay of the solubility of the protein in different detergents and amphiphiles showed high protein-solubility values when either octyl glucoside or lauryldimethylamine-N-oxide was present with heptanetriol or when deoxycholate was present with spermine. The detergent/amphiphile combinations that resulted in high protein solubility were shown to be successful for crystallization of the protein, suggesting that crystallization is favored for detergents and amphiphiles that optimize the solubility of integral membrane proteins. The amphiphiles effective for crystallization were found using laser mass spectrometry to displace the lauryldimethylamine-N-oxide bound to the protein. These results suggest that mass spectrometry can be used for screening of favorable crystallization conditions.

AB - The effect of detergents and amphiphiles on protein solubility and their use in crystallization solutions was examined for an integral membrane protein, the light-harvesting I complex from Rhodospirillum centenum. Measurement by a centrifugation assay of the solubility of the protein in different detergents and amphiphiles showed high protein-solubility values when either octyl glucoside or lauryldimethylamine-N-oxide was present with heptanetriol or when deoxycholate was present with spermine. The detergent/amphiphile combinations that resulted in high protein solubility were shown to be successful for crystallization of the protein, suggesting that crystallization is favored for detergents and amphiphiles that optimize the solubility of integral membrane proteins. The amphiphiles effective for crystallization were found using laser mass spectrometry to displace the lauryldimethylamine-N-oxide bound to the protein. These results suggest that mass spectrometry can be used for screening of favorable crystallization conditions.

UR - http://www.scopus.com/inward/record.url?scp=0042068088&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0042068088&partnerID=8YFLogxK

U2 - 10.1107/S0907444903011909

DO - 10.1107/S0907444903011909

M3 - Article

C2 - 12876344

AN - SCOPUS:0042068088

VL - 59

SP - 1422

EP - 1428

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 0907-4449

IS - 8

ER -