Proteins are biochemical molecules that are essential for life processes. Their function is linked to their structure and so it follows an understanding of their structure will assist in an understanding of their function. The predominant method of solving protein structures is X-ray crystallography and for this a protein crystal is required. The process of obtaining a crystal is amongst the phases of the structure determination process with the highest rates of attrition. Analyses are performed throughout this thesis, which are intended to help improve output for this bottleneck. It has been possible to develop a method to determine pH using a spectrophotometer and acid-base indicator in an accurate, rapid and efficient manner. A method for predicting the pH of buffered solutions has also been developed and these predicted pH values are linked to the isoelectric point of a protein sequence. The isoelectric point is in turn used in classification, along with many other features, to determine a protein's propensity to crystallise. Finally, the most prevalent and successful chemical species in crystallisation are explored, compared and linked. These chemicals are used to design a new crystallisation screen
