Conformational stabilization and crystallization of the SecA translocation ATPase from Bacillus subtilis

S. Weinkauf; J. F. Hunt; J. Scheuring; L. Henry; J. Fak; D. B. Oliver; J. Deisenhofer

doi:10.1107/S0907444901001202

Conformational stabilization and crystallization of the SecA translocation ATPase from Bacillus subtilis

S. Weinkauf, J. F. Hunt, J. Scheuring, L. Henry, J. Fak, D. B. Oliver, J. Deisenhofer

Research output: Contribution to journal › Article › peer-review

17 Scopus citations

Abstract

The SecA translocation ATPase acts as a molecular motor which drives the translocation of proteins through bacterial membranes. In doing so it undergoes large conformational changes and this flexibility may hinder crystallization of the protein. Stabilization of this protein's conformation and its crystallization have been achieved using high glycerol concentrations.

Original language	English (US)
Pages (from-to)	559-565
Number of pages	7
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	57
Issue number	4
DOIs	https://doi.org/10.1107/S0907444901001202
State	Published - 2001

ASJC Scopus subject areas

Structural Biology

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10.1107/S0907444901001202

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title = "Conformational stabilization and crystallization of the SecA translocation ATPase from Bacillus subtilis",

abstract = "The SecA translocation ATPase acts as a molecular motor which drives the translocation of proteins through bacterial membranes. In doing so it undergoes large conformational changes and this flexibility may hinder crystallization of the protein. Stabilization of this protein's conformation and its crystallization have been achieved using high glycerol concentrations.",

author = "S. Weinkauf and Hunt, {J. F.} and J. Scheuring and L. Henry and J. Fak and Oliver, {D. B.} and J. Deisenhofer",

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AU - Weinkauf, S.

AU - Hunt, J. F.

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AU - Henry, L.

AU - Fak, J.

AU - Oliver, D. B.

AU - Deisenhofer, J.

PY - 2001

Y1 - 2001

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AB - The SecA translocation ATPase acts as a molecular motor which drives the translocation of proteins through bacterial membranes. In doing so it undergoes large conformational changes and this flexibility may hinder crystallization of the protein. Stabilization of this protein's conformation and its crystallization have been achieved using high glycerol concentrations.

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Conformational stabilization and crystallization of the SecA translocation ATPase from Bacillus subtilis

Abstract

ASJC Scopus subject areas

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