In:
Acta Crystallographica Section F Structural Biology and Crystallization Communications, International Union of Crystallography (IUCr), Vol. 68, No. 7 ( 2012-07-01), p. 839-841
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.
Type of Medium:
Online Resource
ISSN:
1744-3091
DOI:
10.1107/S1744309112023603
Language:
Unknown
Publisher:
International Union of Crystallography (IUCr)
Publication Date:
2012
detail.hit.zdb_id:
2175956-X
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