title: It's all in the crystals….
abstract: Macromolecular crystallography relies on the availability and quality of single crystals; these are typically obtained through extensive screening, which has a very low intrinsic success rate. Crystallization is not a completely stochastic process and many proteins do not succumb to crystallization because of specific microscopic features of their molecular surfaces. It follows that rational surface engineering through site-directed mutagenesis should allow a systematic and significant improvement in crystallization success rates. Here, one such established strategy, surface-entropy reduction (SER), is discussed, including its successes, limitations and possible future developments.
authors: Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia 22908-0793, USA. zsd4n@virginia.edu
authors: Zygmunt S
authors: ZS
authors: Derewenda
mesh_terms: D018360:Crystallography, X-Ray / Q000379:methods*; D019277:Entropy; D004926:Escherichia coli / Q000737:chemistry; D008958:Models, Molecular; D009154:Mutation; D020836:Protein Structure, Quaternary; D011506:Proteins / Q000032:analysis* / Q000737:chemistry / Q000235:genetics; D013499:Surface Properties
chemical_list: D011506:Proteins