Enhancing protein crystallization through precipitant synergy.

Printer-friendly versionPrinter-friendly versionPDF versionPDF version
TitleEnhancing protein crystallization through precipitant synergy.
Publication TypeJournal Article
Year of Publication2003
AuthorsMajeed, S, Ofek, GA, Belachew, A, Huang, C-chin, Zhou, T, Kwong, PD
JournalStructure
Volume11
Issue9
Pagination1061-70
Date Published2003 Sep
ISSN0969-2126
KeywordsAnimals, Chemical Precipitation, Chickens, Crystallization, Crystallography, X-Ray, Models, Molecular, Muramidase, Protein Conformation, Proteins
Abstract

Suitable conditions for protein crystallization are commonly identified by screening combinations of independent factors that affect crystal formation. Because precipitating agents are prime determinants of crystallization, we investigated whether a systematic exploration of combinations of mechanistically distinct precipitants would enhance crystallization. A crystallization screen containing 64 precipitant mixtures was devised. Tests with ten HIV envelope-related proteins demonstrated that use of precipitant mixtures significantly enhanced both the probability of crystallization as well as the quality of optimized crystals. Tests with hen egg white lysozyme generated a novel C2 crystal from a salt/organic solvent mixture; structure solution at 2 A resolution revealed a lattice held together by both hydrophobic and electrostatic dyad interactions. The results indicate that mechanistically distinct precipitants can synergize, with precipitant combinations adding unique dimensions to protein crystallization.

Alternate JournalStructure
PubMed ID12962625