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Filament-like DREP4 CIDE domain: characterization and preliminary X-ray crystallographic studies.

ABSTRACT: DREP4 is a nuclease from fruit fly that is involved in apoptotic DNA fragmentation. DREP4 contains a conserved CIDE domain that acts as a protein-interaction module and is critical for its function. In this study, it was found that DREP4 CIDE domains form filament-like structures in solution. The length of the highly ordered filament-like structure is dependent on the salt concentration. By adjusting the salt concentration the DREP4 CIDE domain could be crystallized, and X-ray diffraction data were collected to a resolution of 1.9?Å. The crystals were found to belong to the orthorhombic space group P212121, with unit-cell parameters a = 53.08, b = 76.58, c = 174.59?Å.

SUBMITTER: Park HH

PROVIDER: S-EPMC5544006 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature

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Filament-like DREP4 CIDE domain: characterization and preliminary X-ray crystallographic studies.

Park Hyun Ho HH

Acta crystallographica. Section F, Structural biology communications 20170726 Pt 8

DREP4 is a nuclease from fruit fly that is involved in apoptotic DNA fragmentation. DREP4 contains a conserved CIDE domain that acts as a protein-interaction module and is critical for its function. In this study, it was found that DREP4 CIDE domains form filament-like structures in solution. The length of the highly ordered filament-like structure is dependent on the salt concentration. By adjusting the salt concentration the DREP4 CIDE domain could be crystallized, and X-ray diffraction data w ...[more]

PMID: 28777092

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