Crystallization and preliminary X-ray analysis of the complex of the ε-subunit and the central domain of the γ-subunit from the Escherichia coli ATP synthase

A. Rodgers; G. Ewart; G. Cox; M. Wilce

doi:10.1107/S0907444901003018

Crystallization and preliminary X-ray analysis of the complex of the ε-subunit and the central domain of the γ-subunit from the Escherichia coli ATP synthase

A. Rodgers, G. Ewart, G. Cox, M. Wilce^*

^*Corresponding author for this work

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

Abstract

A complex of the ε-subunit and the central domain of the γ-subunit from the ATP synthase of Escherichia coli has been purified and crystallized and preliminary X-ray analysis has been carried out. The crystals belong to space group C222₁, with unit-cell parameters a = 76.7, b = 176.1, c = 67.1 Å (at 100 K). Determination of the structure of this protein complex promises to greatly improve the understanding of energy coupling between the F₀ and F₁ sectors within the enzyme complex.

Original language	English
Pages (from-to)	722-724
Number of pages	3
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	57
Issue number	5
DOIs	https://doi.org/10.1107/S0907444901003018
Publication status	Published - 2001
Externally published	Yes

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title = "Crystallization and preliminary X-ray analysis of the complex of the ε-subunit and the central domain of the γ-subunit from the Escherichia coli ATP synthase",

abstract = "A complex of the ε-subunit and the central domain of the γ-subunit from the ATP synthase of Escherichia coli has been purified and crystallized and preliminary X-ray analysis has been carried out. The crystals belong to space group C2221, with unit-cell parameters a = 76.7, b = 176.1, c = 67.1 {\AA} (at 100 K). Determination of the structure of this protein complex promises to greatly improve the understanding of energy coupling between the F0 and F1 sectors within the enzyme complex.",

author = "A. Rodgers and G. Ewart and G. Cox and M. Wilce",

year = "2001",

doi = "10.1107/S0907444901003018",

language = "English",

volume = "57",

pages = "722--724",

journal = "Acta Crystallographica Section D: Biological Crystallography",

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publisher = "John Wiley \& Sons Inc.",

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TY - JOUR

T1 - Crystallization and preliminary X-ray analysis of the complex of the ε-subunit and the central domain of the γ-subunit from the Escherichia coli ATP synthase

AU - Rodgers, A.

AU - Ewart, G.

AU - Cox, G.

AU - Wilce, M.

PY - 2001

Y1 - 2001

N2 - A complex of the ε-subunit and the central domain of the γ-subunit from the ATP synthase of Escherichia coli has been purified and crystallized and preliminary X-ray analysis has been carried out. The crystals belong to space group C2221, with unit-cell parameters a = 76.7, b = 176.1, c = 67.1 Å (at 100 K). Determination of the structure of this protein complex promises to greatly improve the understanding of energy coupling between the F0 and F1 sectors within the enzyme complex.

AB - A complex of the ε-subunit and the central domain of the γ-subunit from the ATP synthase of Escherichia coli has been purified and crystallized and preliminary X-ray analysis has been carried out. The crystals belong to space group C2221, with unit-cell parameters a = 76.7, b = 176.1, c = 67.1 Å (at 100 K). Determination of the structure of this protein complex promises to greatly improve the understanding of energy coupling between the F0 and F1 sectors within the enzyme complex.

UR - https://www.scopus.com/pages/publications/0035018387

U2 - 10.1107/S0907444901003018

DO - 10.1107/S0907444901003018

M3 - Article

SN - 0907-4449

VL - 57

SP - 722

EP - 724

JO - Acta Crystallographica Section D: Biological Crystallography

JF - Acta Crystallographica Section D: Biological Crystallography

IS - 5

ER -

Crystallization and preliminary X-ray analysis of the complex of the ε-subunit and the central domain of the γ-subunit from the Escherichia coli ATP synthase

Abstract

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