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Crystallization and preliminary X‐ray crystallographic analysis of the XoGroEL chaperonin from Xanthomonas oryzae pv. oryzae
Author(s) -
Tran HuyenThi,
Pham TanViet,
Ngo HoPhuongThuy,
Hong MyoungKi,
Kim JeongGu,
Lee Sang Hee,
Ahn YehJin,
Kang LinWoo
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14006591
Subject(s) - chaperonin , xanthomonas oryzae , groel , crystallization , crystallography , xanthomonas oryzae pv. oryzae , orthorhombic crystal system , groes , protein folding , chemistry , biology , gene , biochemistry , crystal structure , escherichia coli , organic chemistry
Along with the co‐chaperonin GroES, the chaperonin GroEL plays an essential role in enhancing protein folding or refolding and in protecting proteins against misfolding and aggregation in the cellular environment. The XoGroEL gene ( XOO_4288 ) from Xanthomonas oryzae pv. oryzae was cloned and the protein was expressed, purified and crystallized. The purified XoGroEL protein was crystallized using the hanging‐drop vapour‐diffusion method and a crystal diffracted to a resolution of 3.4 Å. The crystal belonged to the orthorhombic space group P 2 1 2 1 2 1 with 14 monomers in the asymmetric unit, with a corresponding V M of 2.7 Å 3 Da −1 and a solvent content of 54.5%.