Crystallization and preliminary X-ray crystallographic analysis of MinE, the cell-division topological specificity factor from Helicobacter pylori

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 May 1;66(Pt 5):527-9. doi: 10.1107/S1744309110009784. Epub 2010 Apr 29.

Abstract

Cell division in Gram-negative bacteria is driven by the formation of an FtsZ ring at the division site. MinE regulates the proper placement of the FtsZ ring at mid-cell by blocking the inhibitory action of the MinCD complex. Diffraction data were collected at 2.8 A resolution from a native crystal of full-length Helicobacter pylori MinE. The crystal belonged to space group P6(4). Assuming the presence of two molecules in the asymmetric unit, the calculated Matthews coefficient was 2.58 A(3) Da(-1), which corresponds to a solvent content of 52.3%. For MAD phasing, a four-wavelength data set was collected at 3.0 A resolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Cell Cycle Proteins / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Helicobacter pylori / chemistry*

Substances

  • Bacterial Proteins
  • Cell Cycle Proteins