Cloning, purification and preliminary X-ray analysis of the C-terminal domain of Helicobacter pylori MotB.

ABSTRACT: The C-terminal domain of MotB (MotB-C) contains a putative peptidoglycan-binding motif and is believed to anchor the MotA/MotB stator unit of the bacterial flagellar motor to the cell wall. Crystals of Helicobacter pylori MotB-C (138 amino-acid residues) were obtained by the hanging-drop vapour-diffusion method using polyethylene glycol as a precipitant. These crystals belong to space group P2(1), with unit-cell parameters a = 50.8, b = 89.5, c = 66.3 A, beta = 112.5 degrees . The crystals diffract X-rays to at least 1.6 A resolution using a synchrotron-radiation source. Self-rotation function and Matthews coefficient calculations suggest that the asymmetric unit contains one tetramer with 222 point-group symmetry. The anomalous difference Patterson maps calculated for an ytterbium-derivative crystal using diffraction data at a wavelength of 1.38 A showed significant peaks on the v = 1/2 Harker section, suggesting that ab initio phase information could be derived from the MAD data.

SUBMITTER: Roujeinikova A 

PROVIDER: S-EPMC2374257 | biostudies-literature | 2008 Apr

REPOSITORIES: biostudies-literature