Expression, purification, crystallization and preliminary X-ray diffraction analysis of alpha-11 giardin from Giardia lamblia.

Acta Crystallogr Sect F Struct Biol Cryst Commun

Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, USA.

Published: November 2006

AI Article Synopsis

  • Alpha-11 Giardin is a protein from the Giardia lamblia parasite, known to cause giardiasis, a type of diarrhea.
  • The study focuses on cloning, expressing, purifying, and crystallizing this protein under two different conditions, resulting in crystals that diffracted at different resolutions.
  • Understanding the atomic structure of alpha-11 giardin may reveal its biological function and help assess its potential as a drug target for treating giardiasis.

Article Abstract

Alpha-11 Giardin, a protein from the annexin superfamily, is a 35.0 kDa protein from the intestinal protozoan parasite Giardia lamblia which triggers a form of diarrhea called giardiasis. Here, the cloning, expression, purification and the crystallization of alpha-11 giardin under two different conditions and in two different space groups is reported. Crystals from the first condition diffracted to 1.1 A and belong to a primitive orthorhombic space group, while crystals from the second condition, which included calcium in the crystallization solution, diffracted to 2.93 A and belong to a primitive monoclinic space group. Determination of the detailed atomic structure of alpha-11 giardin will provide a better insight into its biological function and might establish whether this class of proteins is a potential drug target against giardiasis.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2225204PMC
http://dx.doi.org/10.1107/S1744309106039650DOI Listing

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