Crystallization and preliminary X-ray analysis of phosphoporin from the outer membrane of Escherichia coli

A D Tucker; S Jackman; M W Parker; D Tsernoglou

doi:10.1016/0022-2836(91)90582-q

Crystallization and preliminary X-ray analysis of phosphoporin from the outer membrane of Escherichia coli

J Mol Biol. 1991 Dec 20;222(4):881-4. doi: 10.1016/0022-2836(91)90582-q.

Authors

A D Tucker¹, S Jackman, M W Parker, D Tsernoglou

Affiliation

¹ European Molecular Biology Laboratory, Heidelberg, Germany.

PMID: 1722257
DOI: 10.1016/0022-2836(91)90582-q

Abstract

Phosphoporin is a pore-forming transmembrane protein that spans the outer membrane of Escherichia coli and facilitates the diffusion of phosphates and phosphorylated compounds. Phosphoporin has been crystallized in several different crystal forms, although only one appears to be suitable for X-ray analysis. These crystals, which are hexagonal plates, diffract X-rays to 3 A resolution and belong to the space-group P6(3)22, with unit cell dimensions a = b = 121 A and c = 111 A.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacterial Outer Membrane Proteins / chemistry*
Bacterial Outer Membrane Proteins / isolation & purification
Crystallization
Escherichia coli / chemistry*
Ion Channels / chemistry
Porins
Protein Conformation
X-Ray Diffraction / methods

Substances

Bacterial Outer Membrane Proteins
Ion Channels
Porins