Crystallization and preliminary X-ray crystallographic studies of the native and chemically modified anion-selective porin from Comamonas acidovorans

Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):650-3. doi: 10.1107/s0907444997018854.

Abstract

Omp32, the strongly anion-selective porin from Comamonas acidovorans, has been crystallized. Two crystal forms were observed, both of which belong to space group R3, but exhibit different cell dimensions a = b = 106.7, c = 140.6 A (crystal form I) and a = b = 87.1, c = 135.3 A (crystal form II) with one trimer per asymmetric unit. The crystals diffract to 2.2 and 2.3 A resolution, respectively. Omp32 was chemically modified by introducing negative charges through succinylation. The number and positions of the individual modifications were determined using mass spectrometry and X-ray crystallography. Chemically modified porins yielded crystals of a third form, also of space group R3 but with cell constants of a = b = 109.3 and c = 263.2 A (crystal form III), showing a virtually doubled c axis. Crystals of form III diffract to 3.5 A resolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification
  • Crystallization
  • Crystallography, X-Ray
  • Gram-Negative Bacteria / chemistry*
  • Porins / chemistry*
  • Porins / isolation & purification
  • Protein Conformation
  • Scattering, Radiation
  • Spectroscopy, Fourier Transform Infrared

Substances

  • Bacterial Proteins
  • Omp32 protein, bacteria
  • Porins