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

Autor: Jean Jakoncic, Bruce J. Hrnjez, Sergey V. Buldyrev, Neer Asherie, Dahniel Sastow, Jerome M. Karp, Ariel Axelbaum, Jacob Berger, Mark Stauber
Rok vydání: 2014
Předmět:
Zdroj: Acta Crystallographica Section D: Biological Crystallography
ISSN: 1399-0047
Popis: Crystallization of lysozyme with (R)-2-methyl-2,4-pentanediol produces more ordered crystals and a higher resolution protein structure than crystallization with (S)-2-methyl-2,4-pentanediol. The results suggest that chiral interactions with chiral additives are important in protein crystal formation.
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.
Databáze: OpenAIRE