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- W2016861207 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 C 2, with unit-cell parameters a = 109.1, b = 126.0, c = 83.3 Å, β = 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." @default.
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- W2016861207 date "2012-06-28" @default.
- W2016861207 modified "2023-09-24" @default.
- W2016861207 title "Expression, purification, crystallization and preliminary X-ray diffraction analysis of Deg5 from<i>Arabidopsis thaliana</i>" @default.
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- W2016861207 doi "https://doi.org/10.1107/s1744309112023603" @default.
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