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Crystallization and preliminary X-ray analysis of the FliH–FliI complex responsible for bacterial flagellar type III protein export
Description
<jats:p>The bacterial flagellar proteins are translocated into the central channel of the flagellum by a specific protein-export apparatus for self-assembly at the distal growing end. FliH and FliI are soluble components of the export apparatus and form an FliH<jats:sub>2</jats:sub>–FliI heterotrimer in the cytoplasm. FliI is an ATPase and the FliH<jats:sub>2</jats:sub>–FliI complex delivers export substrates from the cytoplasm to an export gate made up of six integral membrane proteins of the export apparatus. In this study, an FliH<jats:sub>C</jats:sub>fragment consisting of residues 99–235 was co-purified with FliI and the FliH<jats:sub>C2</jats:sub>–FliI complex was crystallized. Crystals were obtained using the hanging-drop vapour-diffusion technique with PEG 400 as a precipitant. The crystals belonged to the orthorhombic space group<jats:italic>P</jats:italic>2<jats:sub>1</jats:sub>2<jats:sub>1</jats:sub>2<jats:sub>1</jats:sub>, with unit-cell parameters<jats:italic>a</jats:italic>= 133.7,<jats:italic>b</jats:italic>= 147.3,<jats:italic>c</jats:italic>= 164.2 Å, and diffracted to 3.0 Å resolution.</jats:p>
Journal
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- Acta Crystallographica Section F Structural Biology and Crystallization Communications
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Acta Crystallographica Section F Structural Biology and Crystallization Communications 68 (11), 1311-1314, 2012-10-30
International Union of Crystallography (IUCr)