Crystallization and preliminary crystallographic data for fructose-1,6-bisphosphate aldolase from Drosophila melanogaster.
Copyright policy )Crystallization and preliminary crystallographic data for fructose-1,6-bisphosphate aldolase from Drosophila melanogaster.
Fructose-1,6-bisphosphate aldolase from Drosophila melanogaster has been crystallized from polyethylene glycol 6000 by vapor diffusion technique against buffered polyethylene glycol solutions at 2-4 degrees C. The insect enzyme crystallizes in the orthorhombic system, heretofore unknown for aldolases. The crystals have the space group P212121 (a = 86.3 A, b = 115.7 A, and c = 151.4 A) and contain four tetrameric aldolase molecules, each with Mr = 158,000/unit cell, i.e. one tetramer/asymmetric unit. The crystals are quite stable to x-ray deterioration. This stability may be related to the unusually low cysteine and histidine content of Drosophila aldolase.
Drosophila melanogaster, Species Specificity, X-Ray Diffraction, Protein Conformation, Fructose-Bisphosphate Aldolase, Muscles, Animals, Humans, Rabbits, Crystallization
Drosophila melanogaster, Species Specificity, X-Ray Diffraction, Protein Conformation, Fructose-Bisphosphate Aldolase, Muscles, Animals, Humans, Rabbits, Crystallization
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