Crystallization and preliminary crystallographic studies of MOMP (major outer membrane protein) from Campylobacter jejuni

Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 2):2349-51. doi: 10.1107/S0907444904024795. Epub 2004 Nov 26.

Abstract

Campylobacter jejuni is the leading bacterial cause of human enteritis linked to ingestion of contaminated food or water. MOMP, the major outer membrane protein from these Gram-negative bacteria, belongs to the porin family. In order to determine the three-dimensional structure of this protein and to elucidate the underlying molecular mechanisms, the MOMP from C. jejuni strain 85H has been purified and crystallized by vapour diffusion. Two crystal forms were characterized for this membrane protein. X-ray diffraction data were collected to a resolution of 3.1 A using a synchrotron-radiation source from the orthorhombic crystal form, which belonged to space group P2(1)2(1)2 with unit-cell parameters a = 170.1, b = 101.9, c = 104.9 A. With a trimer in the asymmetric unit, the solvent content is 64% (V(M) = 3.4 A Da(-1)). The other form exhibits trigonal symmetry (space group R3) with hexagonal unit-cell parameters a = b = 94.2, c = 161.2 A, but diffracts X-rays poorly to about 4 A with significant anisotropy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Campylobacter jejuni / metabolism*
  • Crystallization
  • Crystallography, X-Ray / methods*
  • Dimerization
  • Kinetics
  • Membrane Proteins / chemistry
  • Porins / chemistry*
  • Porins / metabolism
  • Protein Conformation
  • Synchrotrons
  • Temperature
  • X-Ray Diffraction

Substances

  • Bacterial Proteins
  • Membrane Proteins
  • Porins
  • major outer membrane protein, Campylobacter jejuni