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

Crystallization and preliminary X‐ray diffraction analysis of the lytic transglycosylase MltE from Escherichia coli

Buy Article:

$52.00 + tax (Refund Policy)

MltE from Escherichia coli (193 amino acids, 21 380 Da) is a lytic transglycosylase that initiates the first step of cell‐wall recycling. This enzyme is responsible for the cleavage of the cell‐wall peptidoglycan at the β‐1,4‐glycosidic bond between the N‐acetylglucosamine and N‐acetylmuramic acid units. At the end this reaction generates a disaccharide that is internalized and initiates the recycling process. To obtain insights into the biological functions of MltE, crystallization trials were performed and crystals of MltE protein that were suitable for X‐ray diffraction analysis were obtained. The MltE protein of E. coli was crystallized using the hanging‐drop vapour‐diffusion method at 291 K. Crystals grew from a mixture consisting of 28% polyethylene glycol 4000, 0.1 M Tris pH 8.4 and 0.2 M magnesium chloride. Further optimization was performed using the microbatch technique. Single crystals were obtained that belonged to the orthorhombic space group C2221, with unit‐cell parameters a = 123.32, b = 183.93, c = 35.29 Å, and diffracted to a resolution of 2.1 Å.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: Escherichia coli; MltE; cell‐wall recycling; lytic transglycosylases

Document Type: Research Article

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