Open AccessAn improved strategy for the crystallization of Leishmania mexicana pyruvate kinase
Author(s) -
Morgan Hugh P.,
McNae Iain W.,
Hsin KunYi,
Michels Paul A. M.,
FothergillGilmore Linda A.,
Walkinshaw Malcolm D.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109053494
Subject(s) - crystallization , molecule , intermolecular force , macromolecule , crystal (programming language) , crystallography , crystal structure , protein crystallization , chemistry , materials science , biochemistry , organic chemistry , computer science , programming language
The inclusion of novel small molecules in crystallization experiments has provided very encouraging results and this method is now emerging as a promising alternative strategy for crystallizing `problematic' biological macromolecules. These small molecules have the ability to promote lattice formation through stabilizing intermolecular interactions in protein crystals. Here, the use of 1,3,6,8‐pyrenetetrasulfonic acid (PTS), which provides a helpful intermolecular bridge between Leishmania mexicana PYK ( Lm PYK) macromolecules in the crystal, is reported, resulting in the rapid formation of a more stable crystal lattice at neutral pH and greatly improved X‐ray diffraction results. The refined structure of the Lm PYK–PTS complex revealed the negatively charged PTS molecule to be stacked between positively charged (surface‐exposed) arginine side chains from neighbouring Lm PYK molecules in the crystal lattice.