Cloning, purification and preliminary X-ray analysis of the C-terminal domain of Helicobacter pylori MotB.
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.
Roujeinikova
Anna
A
Manchester Interdisciplinary Biocentre, Faculty of Life Sciences, University of Manchester, 131 Princess Street, Manchester M1 7DN, England. anna.roujeinikova@manchester.ac.uk
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D016480:Helicobacter pylori / Q000737:chemistry* / Q000235:genetics*; D017434:Protein Structure, Tertiary / Q000235:genetics
D001426:Bacterial Proteins; C064779:MotB protein, Bacteria