Dramatic improvement of crystal quality for low-temperature-grown rabbit muscle aldolase.
Rabbit muscle aldolase (RMA) was crystallized in complex with the low-complexity domain (LC4) of sorting nexin 9. Monoclinic crystals were obtained at room temperature that displayed large mosaicity and poor X-ray diffraction. However, orthorhombic RMA-LC4 crystals grown at 277 K under similar conditions exhibited low mosaicity, allowing data collection to 2.2 A Bragg spacing and structure determination. It was concluded that the improvement of crystal quality as indicated by the higher resolution of the new RMA-LC4 complex crystals was a consequence of the introduction of new lattice contacts at lower temperature. The lattice contacts corresponded to an increased number of interactions between high-entropy side chains that mitigate the lattice strain incurred upon cryocooling and accompanying mosaic spread increases. The thermodynamically unfavorable immobilization of high-entropy side chains used in lattice formation was compensated by an entropic increase in the bulk-solvent content owing to the greater solvent content of the crystal lattice.
Park
Hajeung
H
Cell Adhesion Laboratory, Department of Cancer Biology, The Scripps Research Institute, Jupiter, FL 33458, USA.
Rangarajan
Erumbi S
ES
Sygusch
Jurgen
J
Izard
Tina
T
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D005634:Fructose-Bisphosphate Aldolase / Q000737:chemistry*; D008958:Models, Molecular; D018482:Muscle, Skeletal / Q000201:enzymology*; D017434:Protein Structure, Tertiary; D011817:Rabbits; D013696:Temperature; D013816:Thermodynamics
D005634:Fructose-Bisphosphate Aldolase
J Biol Chem. 2010 Apr 16;285(16):11983-90
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