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pubmed-article:12962625pubmed:abstractTextSuitable 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.lld:pubmed
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pubmed-article:12962625pubmed:dateRevised2009-11-19lld:pubmed
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pubmed-article:12962625pubmed:articleTitleEnhancing protein crystallization through precipitant synergy.lld:pubmed
pubmed-article:12962625pubmed:affiliationVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.lld:pubmed
pubmed-article:12962625pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:12962625pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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