title: 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, 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.
authors: Laboratory of Noncoding RNA, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, People's Republic of China.
authors: Haitian
authors: H
authors: Fan
authors: Wei
authors: W
authors: Sun
authors: Zhe
authors: Z
authors: Sun
authors: Feng
authors: F
authors: Gao
authors: Weimin
authors: W
authors: Gong
mesh_terms: D017360:Arabidopsis / Q000201:enzymology*; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D015870:Gene Expression; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
chemical_list: D029681:Arabidopsis Proteins; C436319:SPPA protein, Arabidopsis; D012697:Serine Endopeptidases