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Title: Crystallization and preliminary crystallographic data for fructose-1,6-bisphosphate aldolase from Drosophila melanogaster. Author: Brenner-Holzach O, Smit JD. Journal: J Biol Chem; 1982 Oct 10; 257(19):11747-9. PubMed ID: 6811586. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]