CPPS Volume 8, Number 2, April 2007
This issue of Current Protein and Peptide Science is devoted to the emerging field of likelihood of protein crystallization and is related to the seminars and lectures presented recently at the Workshop on the definition of protein domains and their likelihood of crystallization, held in Vienna at the end of June 2006 (http://www.embl-hamburg.de/workshops/2006/domains/), where a number of scientists addressed these questions by presenting and debating both experimental and computational approaches.
Likelihood of crystallization must be predicted computationally and/or determined experimentally in order to avoid time expensive experiments on samples, the three-dimensional structure of which cannot be determined experimentally, because of a series of possible obstacles. For example, if a protein is natively disordered, in the sense that it is not characterized by a unique, well defined conformation, its three-dimensional structure cannot be determined experimentally, since it does not exist. Moreover, a sequence construct that does not correspond to a protein domain might be difficult to express because of its misfolding or its reduced solubility.
This is particularly important in the structural genomics era, in which high throughput approaches are applied to the determination of three-dimensional structures of proteins, the biochemical, biophysical, and biological features of which were not previously studied. However, the preliminary analysis and estimation of the likelihood of crystallization is not relegated to proteomics studies only, but it is important also for traditional hypothesis driven projects, in which the optimization of the protein sample is equally important, allowing one to generate samples suitable for structural studies and/or improve diffraction quality of crystals and obtain, as a consequence, more reliable final results.
Details of this special issue are available on http://www.bentham.org/cpps/