Crystallization of lysozyme with (R)-, (S)- and (RS)-2-methyl-2,4-pentanediol.

ABSTRACT: Chiral control of crystallization has ample precedent in the small-molecule world, but relatively little is known about the role of chirality in protein crystallization. In this study, lysozyme was crystallized in the presence of the chiral additive 2-methyl-2,4-pentanediol (MPD) separately using the R and S enantiomers as well as with a racemic RS mixture. Crystals grown with (R)-MPD had the most order and produced the highest resolution protein structures. This result is consistent with the observation that in the crystals grown with (R)-MPD and (RS)-MPD the crystal contacts are made by (R)-MPD, demonstrating that there is preferential interaction between lysozyme and this enantiomer. These findings suggest that chiral interactions are important in protein crystallization.

SUBMITTER: Stauber M 

PROVIDER: S-EPMC4356360 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature