Production and Crystallization of Protein Domains: How Useful are Disorder Predictions ?

Title: Production and Crystallization of Protein Domains: How Useful are Disorder Predictions ?

Volume: 8 Issue: 2

Author(s): S. Quevillon-Cheruel, Nicolas Leulliot, Lucie Gentils, Herman van Tilbeurgh and Anne Poupon

Affiliation:

Keywords: Protein domain, disorder prediction, protein expression, crystallization

Abstract: The failure to produce and/or crystallize proteins is often due to their modular structure. There exists therefore considerable interest to develop strategies for tailoring proteins into crystallizable domains. In the framework of a Structural Genomics Project on soluble yeast proteins, we have tested the expression of numerous genetic constructs of our targets in order to produce and crystallize proteins and protein domains and solve their three-dimensional structure. In some cases, the choice of the domain boundaries was guided by prediction from sequence using various software packages, including Prelink, a home-made prediction method for detecting unfolded regions. In other cases, large numbers of constructs were generated using molecular biology or biochemical methods. In this paper, we analyze the results of the over-expression in E. coli and crystallization of these constructs, and compare these with the predictions that can be obtained from our software and from others.

Cite this article as:

Quevillon-Cheruel S., Leulliot Nicolas, Gentils Lucie, van Tilbeurgh Herman and Poupon Anne, Production and Crystallization of Protein Domains: How Useful are Disorder Predictions ?, Current Protein & Peptide Science 2007; 8 (2) . https://dx.doi.org/10.2174/138920307780363433