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Purification and crystallization of the entire recombinant subunit E of the energy producer A 1 A o ATP synthase

Purification and crystallization of the entire recombinant subunit E of the energy producer A 1 A... A1Ao ATP synthases are the major energy producers in archaea. Subunit E of the stator domain of the ATP synthase from Pyrococcus horikoshii OT3 was cloned, expressed and purified to homogeneity. The monodispersed protein was crystallized by vapour diffusion. A complete diffraction data set was collected to 3.3 Å resolution with 99.4% completeness using a synchrotron‐radiation source. The crystals belonged to space group I4, with unit‐cell parameters a = 112.51, b = 112.51, c = 96.25 Å, and contained three molecules in the asymmetric unit. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Purification and crystallization of the entire recombinant subunit E of the energy producer A 1 A o ATP synthase

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References (14)

Publisher
Wiley
Copyright
International Union of Crystallography, 2010
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309110001016
pmid
20208172
Publisher site
See Article on Publisher Site

Abstract

A1Ao ATP synthases are the major energy producers in archaea. Subunit E of the stator domain of the ATP synthase from Pyrococcus horikoshii OT3 was cloned, expressed and purified to homogeneity. The monodispersed protein was crystallized by vapour diffusion. A complete diffraction data set was collected to 3.3 Å resolution with 99.4% completeness using a synchrotron‐radiation source. The crystals belonged to space group I4, with unit‐cell parameters a = 112.51, b = 112.51, c = 96.25 Å, and contained three molecules in the asymmetric unit.

Journal

Acta Crystallographica Section FWiley

Published: Mar 1, 2010

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