Crystallization and X-ray crystallographic studies of an inhibitor from rye (Secale cereale) active against Acanthoscelides obtectus and Zabrotes subfasciatus alpha-amylases

Protein Pept Lett. 2004 Feb;11(1):79-83. doi: 10.2174/0929866043478419.

Abstract

Crystals of a new inhibitor present in rye seeds active against alpha-amylases from crop pests Acanthoscelides obtectus and Zabrotes subfasciatus have been obtained. A native dataset was collected at 2.21 A resolution with 99.3% completeness at CPr beamline at LNLS. The crystals belong to the trigonal system, space group P3(1)21 with a=b=78.21 A, and c=59.61 A. The crystal calculated solvent content is compatible with one dimer per asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Coleoptera / enzymology*
  • Crystallization
  • Crystallography, X-Ray
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / isolation & purification
  • Secale / chemistry*
  • alpha-Amylases / antagonists & inhibitors*
  • alpha-Amylases / metabolism

Substances

  • Enzyme Inhibitors
  • alpha-Amylases