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Protein crystallization and initial neutron diffraction studies of the photosystem II subunit PsbO.

ABSTRACT: The PsbO protein of photosystem II stabilizes the active-site manganese cluster and is thought to act as a proton antenna. To enable neutron diffraction studies, crystals of the ?-barrel core of PsbO were grown in capillaries. The crystals were optimized by screening additives in a counter-diffusion setup in which the protein and reservoir solutions were separated by a 1% agarose plug. Crystals were cross-linked with glutaraldehyde. Initial neutron diffraction data were collected from a 0.25?mm3 crystal at room temperature using the MaNDi single-crystal diffractometer at the Spallation Neutron Source, Oak Ridge National Laboratory.

SUBMITTER: Bommer M

PROVIDER: S-EPMC5619745 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature

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Protein crystallization and initial neutron diffraction studies of the photosystem II subunit PsbO.

Bommer Martin M Coates Leighton L Dau Holger H Zouni Athina A Dobbek Holger H

Acta crystallographica. Section F, Structural biology communications 20170831 Pt 9

The PsbO protein of photosystem II stabilizes the active-site manganese cluster and is thought to act as a proton antenna. To enable neutron diffraction studies, crystals of the β-barrel core of PsbO were grown in capillaries. The crystals were optimized by screening additives in a counter-diffusion setup in which the protein and reservoir solutions were separated by a 1% agarose plug. Crystals were cross-linked with glutaraldehyde. Initial neutron diffraction data were collected from a 0.25 mm< ...[more]

PMID: 28876232

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