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

ABSTRACT: A(1)A(o) 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 A 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 A, and contained three molecules in the asymmetric unit.

SUBMITTER: Balakrishna AM

PROVIDER: S-EPMC2833048 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature

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

Balakrishna Asha Manikkoth AM Hunke Cornelia C Grüber Gerhard G

Acta crystallographica. Section F, Structural biology and crystallization communications 20100225 Pt 3

A(1)A(o) 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 A 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 A, and c ...[more]

PMID: 20208172

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