Crystallization of the immunodominant outer membrane protein OmpC; the first protein crystals from Salmonella typhi, a human pathogen

FEBS Lett. 1999 Jun 25;453(3):380-2. doi: 10.1016/s0014-5793(99)00746-2.


OmpC, a surface antigen of Salmonella typhi was crystallized after several attempts, using PEG 3350. Well shaped hexagonal crystals were grown from vapor diffusion method using octyl glucoside and C12E9 as detergents. Crystals are sensitive to X-ray and diffract weakly up to 7 A. Porin isoforms, due to the bound lipopolysaccharides, could be the cause for poor diffraction. Crystal quality depends largely on the purification method, and in case of LPS contamination, the genetic background of the bacteria. Crystallization and initial data collection suggest optimum conditions and the method of choice for OmpC crystallization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigens, Bacterial / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Immunodominant Epitopes / chemistry*
  • Porins / chemistry*
  • Salmonella typhi / immunology*


  • Antigens, Bacterial
  • Immunodominant Epitopes
  • OmpC protein
  • Porins