Open AccessCrystallization of lysozyme with ( R )‐, ( S )‐ and ( RS )‐2‐methyl‐2,4‐pentanediol
Author(s) -
Stauber Mark,
Jakoncic Jean,
Berger Jacob,
Karp Jerome M.,
Axelbaum Ariel,
Sastow Dahniel,
Buldyrev Sergey V.,
Hrnjez Bruce J.,
Asherie Neer
Publication year - 2015
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s1399004714025061
Subject(s) - crystallization , lysozyme , enantiomer , chirality (physics) , protein crystallization , crystallography , molecule , chiral resolution , chemistry , resolution (logic) , crystal (programming language) , stereochemistry , materials science , organic chemistry , chiral symmetry , physics , biochemistry , quantum mechanics , artificial intelligence , computer science , nambu–jona lasinio model , programming language , quark
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.