Related Experiment Video
Updated: Oct 1, 2026

Determining the Ice-binding Planes of Antifreeze Proteins by Fluorescence-based Ice Plane Affinity
Published on: January 15, 2014
Elevated temperature and tyrosine iodination aid in the crystallization and structure determination of an antifreeze
Eeva K Leinala1, Peter L Davies, Zongchao Jia
1Department of Biochemistry, Queen's University, Kingston, Ontario K7L 3N6, Canada.
Abstract:
Production and refolding of recombinant Choristoneura fumiferana antifreeze protein (CfAFP) leads to a disulfide-bonded product containing dynamic conformational microheterogeneity. Difficulties in the crystallization of this protein arising from its microheterogeneity were overcome by screening of crystallization conditions at various temperatures and finally using a temperature of 318 K to obtain diffraction-quality crystals. In addition, heavy-atom derivatization of this protein required the iodination of a specific tyrosine residue, leading to the successful single anomalous scattering (SAS) structure determination. The techniques of higher temperature screening, to reduce dynamic conformational microheterogeneity, and defined tyrosine iodination, for specific heavy-atom incorporation, are methods which can be employed with other proteins to aid in structure determination.
More Related Videos
Related Concept Videos
Phase Transitions: Melting and Freezing
Recrystallization: Solid–Solution Equilibria

