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Expression, purification, crystallization and preliminary X-ray diffraction analysis of Deg5 from Arabidopsis thaliana.

ABSTRACT: Arabidopsis thaliana Deg5 is an ATP-independent serine protease which resides on the luminal side of the thylakoid in chloroplasts. Deg5 and another Deg/HtrA-family protease, Deg8, have a synergistic function in the turnover of the D1 protein of photosystem II (PSII), which is prone to damage arising from high light exposure. An inactive mutant of the protein, Deg5(S266A), was overexpressed in Escherichia coli. After purification and crystallization, crystals that diffracted to 2.6?Å resolution were obtained. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 109.1, b = 126.0, c = 83.3?Å, ? = 102.9°, and contained three molecules in the asymmetric unit. The calculated Matthews coefficient and solvent content were 3.0?Å(3)?Da(-1) and 59.0%, respectively.

SUBMITTER: Fan H

PROVIDER: S-EPMC3388936 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature

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Expression, purification, crystallization and preliminary X-ray diffraction analysis of Deg5 from Arabidopsis thaliana.

Fan Haitian H Sun Wei W Sun Zhe Z Gao Feng F Gong Weimin W

Acta crystallographica. Section F, Structural biology and crystallization communications 20120628 Pt 7

Arabidopsis thaliana Deg5 is an ATP-independent serine protease which resides on the luminal side of the thylakoid in chloroplasts. Deg5 and another Deg/HtrA-family protease, Deg8, have a synergistic function in the turnover of the D1 protein of photosystem II (PSII), which is prone to damage arising from high light exposure. An inactive mutant of the protein, Deg5(S266A), was overexpressed in Escherichia coli. After purification and crystallization, crystals that diffracted to 2.6 Å resolution ...[more]

PMID: 22750879

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