An improved purification of ECF1 and ECF1F0 by using a cytochrome bo- deficient strain of Escherichia coli facilitates crystallization of these complexes

Gerhard Grüber, Andrew Hausrath, Martin Sagermann, Roderick A. Capaldi

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

A novel strategy, which employs a cytochrome bo-lacking strain (GO104) and a modified isolation procedure provides an effective approach for obtaining much purer preparations of ECF1F0 than described previously, as well as for isolating homogeneous and protein-chemically pure ECF1. ECF1 obtained in this way could be crystallized by vapor-diffusion using polyethylene glycol (PEG) as a precipitant in a form suitable for X-ray diffraction analysis. The crystals belong to the orthorhombic space group P212121, with lattice parameters a = 110, b = 134, and c= 269 Å, and diffract to a resolution of at least 6.4 Å.

Original languageEnglish (US)
Pages (from-to)165-168
Number of pages4
JournalFEBS Letters
Volume410
Issue number2-3
DOIs
StatePublished - Jun 30 1997
Externally publishedYes

Fingerprint

Cytochromes
Crystallization
X-Ray Diffraction
X ray diffraction analysis
Escherichia coli
Lattice constants
Purification
Vapors
Crystals
Proteins

Keywords

  • Crystal
  • F-ATPase
  • FF-ATP synthase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

An improved purification of ECF1 and ECF1F0 by using a cytochrome bo- deficient strain of Escherichia coli facilitates crystallization of these complexes. / Grüber, Gerhard; Hausrath, Andrew; Sagermann, Martin; Capaldi, Roderick A.

In: FEBS Letters, Vol. 410, No. 2-3, 30.06.1997, p. 165-168.

Research output: Contribution to journalArticle

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