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

Crystallization and preliminary X‐ray analysis of Thermoactinomyces vulgaris R‐47 maltooligosaccharide‐metabolizing enzyme homologous to glucoamylase

Buy Article:

$52.00 + tax (Refund Policy)

A maltooligosaccharide‐metabolizing enzyme from Thermoactinomyces vulgaris R‐47 (TGA) homologous to glucoamylase degrades maltooligosaccharides more efficiently than starch, unlike fungal glucoamylases. TGA was crystallized and the state of the protein in solution was analyzed by gel‐filtration chromatography. Diffraction data were collected to 3.31 Å resolution. The TGA crystal belongs to the orthorhombic space group P212121 or P21212, with unit‐cell parameters a = 110.2, b = 317.6, c = 144.9 Å, and is expected to contain five to eight TGA molecules per asymmetric unit. Gel‐filtration and native PAGE analyses indicated that TGA exists as a dimer in solution. This is the first report of the crystallization of an oligomeric glucoamylase.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: maltooligosaccharide‐metabolizing enzyme

Document Type: Research Article

Publication date: March 1, 2005

  • 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