Enhancing ubiquitin crystallization through surface-entropy reduction.

ABSTRACT: 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 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 384-condition crystallization screen. The likelihood of obtaining crystals varied by two orders of magnitude within this set of eight protei

SUBMITTER: Loll PJ 

PROVIDER: S-EPMC4188098 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature