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

Crystallization of Escherichia coli maltoporin in the trigonal space group R3

Buy Article:

$52.00 + tax (Refund Policy)

Maltoporin is an outer‐membrane protein that forms a β‐barrel composed of three monomers and ensures the transport of maltose and maltodextrin in Gram‐negative bacteria. Previously, the crystallization of Escherichia coli or Salmonella typhimurium maltoporin has been achieved in the presence of a mixture of the detergents β‐decylmaltoside and dodecyl nonaoxyethylene. These crystals all belonged to the orthorhombic space group C2221 and gave rise to several structures of maltoporin in complex with different carbohydrates determined at resolutions between 3.2 and 2.4 Å. Here, the crystallization of E. coli maltoporin in a new crystal form is reported; the crystals belonged to the trigonal R3 space group and diffracted to 1.9 Å resolution. These crystals were obtained using n‐dodecyl‐β‐d‐maltoside as a detergent. Crystals with a lens or pyramidal morphology could be obtained using sitting or hanging drops, respectively, and despite their very different shapes they presented the same space group and very similar unit‐cell parameters.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: carbohydrates; maltoporin; outer‐membrane proteins

Document Type: Research Article

Affiliations: Centre for Carbohydrate Recognition and Signalling, Department of Molecular Biology, Gustav Wieds 10C, Aarhus University, Aarhus, Denmark

Publication date: January 1, 2011

  • 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