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

摘要

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.