Protein Crystallization and Structure Determination

Our understanding of life at the molecular level is highly dependent on the ability to map the
molecular details of individual proteins and nucleic acids as well as their interactions with each
other and with small molecules (inhibitors, cofactors, substrates, etc.). The determination of
3-D structures of proteins is crucial for the understanding of these interactions as well as their
structure–function relationships, which also has many practical applications in drug design
and protein engineering.

Structure determination is usually a tedious and expensive process whereby the target
macromolecule must be produced in relatively large quantities and purified in high
concentrations. A successful experiment often requires expert knowledge of biochemistry,
bioinformatics and molecular biology. Over the past decades, rapid technical advances in
DNA cloning, protein expression and purification methodologies have made it generally easy
to obtain enough amount of proteins for their structural study. Besides, numerous innovations
and improvements have been made in solving protein structures using instrumental methods
such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy and electron
microscopy (EM). These efforts together have given rise to dramatic accumulation of 3-D
structural data in the past few decades (Figure 1). The large number of protein structures will
certainly yield valuable information to the rules for elucidating protein folding/unfolding
mechanisms and understanding their biological functions.

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