Strategy for membrane protein crystallization exemplified with OmpA and OmpX

Proteins. 1999 Feb 1;34(2):167-72.

Abstract

The bacterial outer membrane proteins OmpA and OmpX were modified in such a manner that they yielded bulky crystals diffracting X-rays isotropically beyond 2 A resolution and permitting detailed structural analyses. The procedure involved semi-directed mutagenesis, mass production into inclusion bodies, and (re)naturation therefrom; it should be applicable for a broader range of membrane proteins.

MeSH terms

  • Bacterial Outer Membrane Proteins / biosynthesis
  • Bacterial Outer Membrane Proteins / chemistry*
  • Bacterial Outer Membrane Proteins / genetics
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / chemistry*
  • Escherichia coli / genetics
  • Escherichia coli Proteins*
  • Hydrolases*
  • Inclusion Bodies / metabolism
  • Mutagenesis
  • Protein Denaturation

Substances

  • Bacterial Outer Membrane Proteins
  • Escherichia coli Proteins
  • OmpX protein, E coli
  • OMPA outer membrane proteins
  • Hydrolases