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Expression, purification, crystallization and preliminary X-ray diffraction analysis of a core fragment of FlgG, a bacterial flagellar rod protein.

ABSTRACT: FlgG is a bacterial flagellar rod protein and constructs the distal rod connecting to the hook. FlgG of Salmonella enterica serovar Typhimurium is a 260-amino-acid protein composed of a folded core region and N- and C-terminal regions that are unfolded in solution. A core fragment of FlgG (FlgG47-227) was expressed, purified and crystallized. Crystals of native and SeMet-labelled FlgG47-227 were obtained by the sitting-drop vapour-diffusion technique with PEG MME 2000 as precipitant. The native crystal belonged to the primitive orthorhombic space group P212121, with unit-cell parameters a = 47.78, b = 68.94, c = 110.57?Å. The SeMet crystal also belonged to space group P212121, with unit-cell parameters a = 47.53, b = 67.04, c = 110.27?Å.

SUBMITTER: Saijo-Hamano Y

PROVIDER: S-EPMC3660898 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature

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Expression, purification, crystallization and preliminary X-ray diffraction analysis of a core fragment of FlgG, a bacterial flagellar rod protein.

Saijo-Hamano Yumiko Y Matsunami Hideyuki H Namba Keiichi K Imada Katsumi K

Acta crystallographica. Section F, Structural biology and crystallization communications 20130430 Pt 5

FlgG is a bacterial flagellar rod protein and constructs the distal rod connecting to the hook. FlgG of Salmonella enterica serovar Typhimurium is a 260-amino-acid protein composed of a folded core region and N- and C-terminal regions that are unfolded in solution. A core fragment of FlgG (FlgG47-227) was expressed, purified and crystallized. Crystals of native and SeMet-labelled FlgG47-227 were obtained by the sitting-drop vapour-diffusion technique with PEG MME 2000 as precipitant. The native ...[more]

PMID: 23695574

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