Skip to main content
padlock icon - secure page this page is secure

Preliminary structural investigations of the Eut‐L shell protein of the ethanolamine ammonia‐lyase metabolosome of Escherichia coli

Buy Article:

$52.00 + tax (Refund Policy)

The ethanolamine ammonia‐lyase microcompartment is composed of five different shell proteins that have been proposed to assemble into symmetrically shaped polyhedral particles of varying sizes. Here, preliminary X‐ray analysis of crystals of the bacterial microcompartment shell protein Eut‐L from Escherichia coli is reported. Cloning, overexpression and purification resulted in highly pure protein that crystallized readily under many different conditions. In all cases the protein forms thin hexagonal plate‐shaped crystals belonging to space group P3 that are of unusually high stability against different solvent conditions. The crystals diffracted to a resolution of 2.0 Å using synchrotron radiation but proved to be radiation‐sensitive. Preparations of heavy‐atom‐derivatized crystals for use in determining the three‐dimensional structure are under way.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: ethanolamine ammonia‐lyase metabolosome; shell proteins

Document Type: Research Article

Publication date: February 1, 2009

  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
X
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more