Philip Evans has creatively exploited techniques of protein crystallography and specific mutagenesis to analyse important biological systems. For phosphofructokinase, the key enzyme in the regulation of glycolysis, his structures of inhibited, activated and unliganded enzymes, coupled with extensive mutagenesis of functionally important residues, beautifully explained its catalytic mechanism and the allosteric control of its activity. His revealing analysis of the vitamin B12 dependent enzyme, methylmalonyl-coA mutase provided a structural explanation of the free-radical mechanism of covalent carbon–carbon bond formation.

Most recently, Philip’s work on proteins which underlie vesicle uptake in cell trafficking has led to an appreciation of the importance of specific peptide binding between the protein domains that promote and control complex formation. Through his generous contributions to the development of publicly available computer programs, he has helped to build protein crystallography into a powerful tool.