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.
D000818:Animals; D003460:Crystallization; D004331:Drosophila melanogaster / Q000201:enzymology*; D005634:Fructose-Bisphosphate Aldolase / Q000302:isolation & purification*; D006801:Humans; D009132:Muscles / Q000201:enzymology; D011487:Protein Conformation; D011817:Rabbits; D013045:Species Specificity; D014961:X-Ray Diffraction
D005634:Fructose-Bisphosphate Aldolase