The deposited structure of PDB entry 4pig coloured by chain and viewed from the front. The deposited structure of PDB entry 4pig coloured by chain and viewed from the side. The deposited structure of PDB entry 4pig coloured by chain and viewed from the top. The deposited structure of PDB entry 4pig coloured by chemically distinct molecules and viewed from the front. The deposited structure of PDB entry 4pig coloured by chemically distinct molecules and viewed from the side. The deposited structure of PDB entry 4pig coloured by chemically distinct molecules and viewed from the top. PDB entry 4pig contains 8 copies of Ubiquitin in assembly 5. This protein is highlighted and viewed from the front.
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Ubiquitin has many attributes suitable for a crystallization chaperone, including high stability and ease of expression. However, ubiquitin contains a high surface density of lysine residues and the doctrine of surface-entropy reduction suggests that However, ubiquitin contains a high surface density of lysine residues and the doctrine of surface-entropy reduction suggests that these lysines will resist participating in packing interactions and thereby impede crystallization. To assess the contributions of these residues to crystallization behavior, each of the seven lysines of ubiquitin was mutated to serine and the corresponding single-site mutant proteins were expressed and purified. The behavior of these seven mutants was then compared with that of the wild-type protein in a condition crystallization screen.
